| Version |
2.5 |
| Creation Date |
2006-08-12 20:21:29 |
| Update Date |
2010-04-19 17:15:22 |
| Accession Number |
HMDB03362 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Chitin |
| Description |
Chitin is an unusual substance as it is a naturally occurring polymer. Its breakdown is conducted by bacteria which have receptors to simple sugars from the decomposition of chitin. If chitin is detected they then produce enzymes to digest the chitin by reducing it to simple sugars and ammonia.
Chitin (IPA: [Kaitin]) is one of the main components in the cell walls of fungi, the exoskeletons of insects and other arthropods, and in some other animals. It is a polysaccharide; it is constructed from units of acetylglucosamine (more completely, N-acetyl-D-glucos-2-amine). These are linked together in beta-1,4 fashion (in a similar manner to the glucose units which form cellulose). In effect chitin may be described as cellulose with one hydroxyl group on each monomer replaced by an acetylamine group. This allows for increased hydrogen bonding between adjacent polymers, giving the polymer increased strength.
A linear polysaccharide of beta-1->4 linked units of acetylglucosamine. It is the second most abundant biopolymer on earth, found especially in insects and fungi. When deacetylated it is called chitosan. |
| Synonyms |
- N-acetyl-D-glucosamine
- Poly 2-Acetamido-2-deoxy-D-glucose
- [1,4-(N-Acetyl-beta-D-glucosaminyl)]n
- [1,4-(N-Acetyl-beta-D-glucosaminyl)]n+1
- beta-1,4-Poly-N-acetyl-D-glucosamine
- N-acetyl-delta-glucosamine
- Poly 2-Acetamido-2-deoxy-delta-glucose
- [1,4-(N-Acetyl-beta-delta-glucosaminyl)]n
- [1,4-(N-Acetyl-beta-delta-glucosaminyl)]n+1
- beta-1,4-Poly-N-acetyl-delta-glucosamine
|
| Chemical IUPAC Name |
N-[(2R,4R,5S)-5-[[(2R,4S,5S)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]methoxymethyl]-2-[[(3S,4R,6R)-5-acetamido-4,6-dihydroxy-2-(hydroxymethyl)oxan-3-yl]methoxymethyl]-4-hydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide |
| Chemical Formula |
C28H49N3O16 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Carbohydrates and Carbohydrate conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- hemiacetal
- primary alcohol
- secondary alcohol
- 1,2-diol
- dialkyl ether
- secondary carboxylic acid amide
- heterocyclic compound
|
| Biofunction |
- Component of Aminosugars metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
683.699 |
| Monoisotopic Molecular Weight |
683.311279 |
| Isomeric SMILES |
CC(=O)NC1[C@H](O)OC(CO)[C@@H](COC[C@@H]2OC(CO)[C@@H](COC[C@@H]3OC(CO)[C@@H](O)[C@H](O)C3NC(C)=O)[C@H](O)C2NC(C)=O)[C@@H]1O |
| Canonical SMILES |
CC(=O)NC1C(O)OC(CO)C(COCC2OC(CO)C(COCC3OC(CO)C(O)C(O)C3NC(C)=O)C(O)C2NC(C)=O)C1O |
| KEGG Compound ID |
C00461  |
| BioCyc ID |
14-N-ACETYL-BETA-D-GLUCOSAMINYLN1  |
| BiGG ID |
2242111  |
| Wikipedia Link |
Chitin  |
| NuGOwiki Link |
HMDB03362  |
| Metagene Link |
HMDB03362  |
| METLIN ID |
6903  |
| PubChem Compound |
453624  |
| PubChem Substance |
599272  |
| ChEBI ID |
17029  |
| CAS Registry Number |
1398-61-4 |
| InChI Identifier |
InChI=1/C28H49N3O16/c1-11(35)29-21-19(9-44-8-15-17(5-33)47-28(42)23(25(15)39)31-13(3)37)45-16(4-32)14(24(21)38)7-43-10-20-22(30-12(2)36)27(41)26(40)18(6-34)46-20/h14-28,32-34,38-42H,4-10H2,1-3H3,(H,29,35)(H,30,36)(H,31,37)/t14-,15-,16?,17?,18?,19+,20+,21?,22?,23?,24+,25+,26-,27-,28-/m1/s1 |
| Synthesis Reference |
Kurita, Keisuke; Koyama, Yoshiyuki; Nishimura, Shinichiro; Kamiya, Mami. Facile preparation of water-soluble chitin from chitosan. Chemistry Letters (1989), (9), 1597-8. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 31.0 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-3.03 [Predicted by ALOGPS]; -5.5 [Predicted by PubChem via XLOGP]; -2.83 [MEYLAN,WM & HOWARD,PH (1995)]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
- Extracellular
|
| Biofluid Location |
Not Available |
| Tissue Location |
| Tissue |
References |
| Fibroblasts |
— |
| Intestine |
— |
| Spleen |
— |
| Testes |
— |
|
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Nakajima M, Atsumi K, Kifune K, Miura K, Kanamaru H: Chitin is an effective material for sutures. Jpn J Surg. 1986 Nov;16(6):418-24. [PubMed
]
- Soule JB, Halverson AL, Becker RB, Pistole MC, Orenstein JM: A patient with acquired immunodeficiency syndrome and untreated Encephalitozoon (Septata) intestinalis microsporidiosis leading to small bowel perforation. Response to albendazole. Arch Pathol Lab Med. 1997 Aug;121(8):880-7. [PubMed
]
- Gheri G, Sgambati E, Thyrion GD, Vichi D, Orlandini GE: The oligosaccharidic content of the glycoconjugates of the prepubertal descended and undescended testis: lectin histochemical study. Ital J Anat Embryol. 2004 Apr-Jun;109(2):69-84. [PubMed
]
- Hatcher VB, Schwarzmann GO, Jeanloz RW, McArthur JW: Changes in the sialic acid concentration in the major cervical glycoprotein from the bonnet monkey (Macaca radiata) during a hormonally induced cycle. Fertil Steril. 1977 Jun;28(6):682-8. [PubMed
]
- Piskun RP, Pentiuk AA, Serkova VK, Polesia TL, Savitskaia EA: [Enterosorbents in the treatment of atherosclerosis] Eksp Klin Farmakol. 1998 Mar-Apr;61(2):69-74. [PubMed
]
- Kawashita M, Nakao M, Minoda M, Kim HM, Beppu T, Miyamoto T, Kokubo T, Nakamura T: Apatite-forming ability of carboxyl group-containing polymer gels in a simulated body fluid. Biomaterials. 2003 Jun;24(14):2477-84. [PubMed
]
- Howling GI, Dettmar PW, Goddard PA, Hampson FC, Dornish M, Wood EJ: The effect of chitin and chitosan on the proliferation of human skin fibroblasts and keratinocytes in vitro. Biomaterials. 2001 Nov;22(22):2959-66. [PubMed
]
- Vasstrand EN, Jensen HB: Affinity chromatography of human saliva lysozyme and effect of pH and ionic strength on lytic activity. Scand J Dent Res. 1980 Jun;88(3):219-28. [PubMed
]
- Collard CD, Montalto MC, Reenstra WR, Buras JA, Stahl GL: Endothelial oxidative stress activates the lectin complement pathway: role of cytokeratin 1. Am J Pathol. 2001 Sep;159(3):1045-54. [PubMed
]
- Shibuya N, Nakamura K, Ogoshi K, Ohta T, Hori Y, Kodama K, Yamamoto M: Modification of mutagenic activities of pro-mutagens by glyco-ursodeoxycholic acid in the Ames assay. Tohoku J Exp Med. 1999 Sep;189(1):1-9. [PubMed
]
- Ishihara C, Yoshimatsu K, Tsuji M, Arikawa J, Saiki I, Tokura S, Azuma I: Anti-viral activity of sulfated chitin derivatives against Friend murine leukaemia and herpes simplex type-1 viruses. Vaccine. 1993;11(6):670-4. [PubMed
]
- Zampini M, Pruzzo C, Bondre VP, Tarsi R, Cosmo M, Bacciaglia A, Chhabra A, Srivastava R, Srivastava BS: Vibrio cholerae persistence in aquatic environments and colonization of intestinal cells: involvement of a common adhesion mechanism. FEMS Microbiol Lett. 2005 Mar 15;244(2):267-73. [PubMed
]
- Xu Y, Olman V, Xu D: Clustering gene expression data using a graph-theoretic approach: an application of minimum spanning trees. Bioinformatics. 2002 Apr;18(4):536-45. [PubMed
]
- Sharaev PN, Strelkov NS, Sannikova AA, Zvorykin IA, Men'shikova NN, Sakhabutdinova EP, Gabdrakhmanova NK: [The method for detection of urinary lysozyme] Klin Lab Diagn. 2001 Apr;(4):52-3. [PubMed
]
- Farnia P, Mohammadi F, Zarifi Z, Tabatabee DJ, Ganavi J, Ghazisaeedi K, Farnia PK, Gheydi M, Bahadori M, Masjedi MR, Velayati AA: Improving sensitivity of direct microscopy for detection of acid-fast bacilli in sputum: use of chitin in mucus digestion. J Clin Microbiol. 2002 Feb;40(2):508-11. [PubMed
]
- Sano H, Matsukubo T, Shibasaki K, Itoi H, Takaesu Y: Inhibition of adsorption of oral streptococci to saliva treated hydroxyapatite by chitin derivatives. Bull Tokyo Dent Coll. 1991 Feb;32(1):9-17. [PubMed
]
- Johnson SM, Pappagianis D: The coccidioidal complement fixation and immunodiffusion-complement fixation antigen is a chitinase. Infect Immun. 1992 Jul;60(7):2588-92. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- N-acetylglucosamine kinase
- Acidic mammalian chitinase precursor
- Chitotriosidase-1 precursor
- Chitinase family protein 3
- Chitinase family protein V2
- Chitinase family protein V1
- cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA
- CHIA protein
- Chitinase, acidic
- Chitinase, acidic
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6316 |
| Enzyme 1 Name |
N-acetylglucosamine kinase |
| Enzyme 1 Synonyms |
- GlcNAc kinase
|
| Enzyme 1 Gene Name |
NAGK |
| Enzyme 1 Protein Sequence |
>N-acetylglucosamine kinase
MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKA
GVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGG
VVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHD
IGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGE
MLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFS
SFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS
|
| Enzyme 1 Number of Residues |
344 |
| Enzyme 1 Molecular Weight |
37376 |
| Enzyme 1 Theoretical pI |
6.18 |
| Enzyme 1 GO Classification |
Not Available |
| Enzyme 1 General Function |
Carbohydrate transport and metabolism |
| Enzyme 1 Specific Function |
Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
6491737  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9UJ70  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NAGK_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1035 bp
ATGGCCGCGATCTATGGGGGTGTAGAGGGGGGAGGCACACGATCCGAGGTCCTTTTAGTC
TCAGAGGATGGGAAGATCCTGGCAGAAGCAGATGGACTGAGCACAAACCACTGGCTGATC
GGGACAGACAAGTGTGTGGAGAGGATCAATGAGATGGTGAACAGGGCCAAACGGAAAGCA
GGGGTGGATCCTCTGGTACCGCTGCGAATTTTGGGCCTATCTCTGAGCGGTGGGGACCAG
GAGGACGCGGGGAGGATCCTGATCGAGGAGCTGAGGGACCGATTTCCCTACCTGAGTGAA
AGCTACTTAATCACCACCGATGCCGCCGGCTCCATCGCCACAGCTACACCGGATGGTGGG
ATTGTGCTCATATCTGGAACAGGCTCCAACTGCAGGCTCATCAACCCTGATGGCTCCGAG
AGTGGCTGCGGCGGCTGGGGCCATATGATGGGTGATGAGGGTTCAGCCTACTGGATCGCA
CACCAAGCAGTGAAAATAGTGTTTGACTCCATTGACAACCTAGAGGCGGCTCCTCATGAT
ATCGGCTACGTCAAACAGGCCATGTTCCACTATTTCCAGGTGCCAGATCGGCTAGGGATA
CTCACTCACCTGTATAGGGACTTTGATAAATGCAGGTTTGCTGGGTTTTGCCGGAAAATT
GCAGAAGGTGCTCAGCAGGGAGACCCCCTTTCCCGCTATATCTTCAGGAAGGCTGGGGAG
ATGCTGGGCAGACACATCGTAGCAGTGTTGCCCGAGATTGACCCGGTCTTGTTCCAGGGC
AAGATTGGACTCCCCATCCTGTGCGTGGGCTCTGTGTGGAAGAGCTGGGAGCTGCTGAAG
GAAGGTTTTCTTTTGGCGCTGACCCAGGGCAGAGAGATCCAGGCTCAGAACTTCTTCTCC
AGCTTCACCCTGATGAAGCTGAGGCACTCCTCCGCTCTGGGTGGGGCCAGCCTAGGGGCC
AGGCACATCGGGCACCTCCTCCCCATGGACTATAGCGCCAATGCCATTGCCTTCTATTCC
TACACCTTTTCCTAG
|
| Enzyme 1 GenBank Gene ID |
AJ242910  |
| Enzyme 1 GeneCard ID |
NAGK  |
| Enzyme 1 GenAtlas ID |
NAGK  |
| Enzyme 1 HGNC ID |
HGNC:17174  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Hinderlich S, Berger M, Schwarzkopf M, Effertz K, Reutter W: Molecular cloning and characterization of murine and human N-acetylglucosamine kinase. Eur J Biochem. 2000 Jun;267(11):3301-8. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6317 |
| Enzyme 2 Name |
Acidic mammalian chitinase precursor |
| Enzyme 2 Synonyms |
- AMCase
- TSA1902
|
| Enzyme 2 Gene Name |
CHIA |
| Enzyme 2 Protein Sequence |
>Acidic mammalian chitinase precursor
MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAG
RQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFI
TSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMV
TAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAY
LNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGI
WAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVW
AIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSS
GGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
|
| Enzyme 2 Number of Residues |
476 |
| Enzyme 2 Molecular Weight |
52271 |
| Enzyme 2 Theoretical pI |
5.63 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Degrades chitin and chitotriose. May participate in the defense against nematodes and other pathogens |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
6467177  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BZP6  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CHIA_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1107 bp
ATGGTTTCTACTCCTGAGAACCGCCAGACTTTCATCACCTCAGTCATCAAATTCCTGCGC
CAGTATGAGTTTGACGGGCTGGACTTTGACTGGGAGTACCCTGGCTCTCGTGGGAGCCCT
CCTCAGGACAAGCATCTCTTCACTGTCCTGGTGCAGGAAATGCGTGAAGCTTTTGAGCAG
GAGGCCAAGCAGATCAACAAGCCCAGGCTGATGGTCACTGCTGCAGTAGCTGCTGGCATC
TCCAATATCCAGTCTGGCTATGAGATCCCCCAACTGTCACAGTACCTGGACTACATCCAT
GTCATGACCTACGACCTCCATGGCTCCTGGGAGGGCTACACTGGAGAGAACAGCCCCCTC
TACAAATACCCGACTGACACCGGCAGCAACGCCTACCTCAATGTGGATTATGTCATGAAC
TACTGGAAGGACAATGGAGCACCAGCTGAGAAGCTCATCGTTGGATTCCCTACCTATGGA
CACAACTTCATCCTGAGCAACCCCTCCAACACTGGAATTGGTGCCCCCACCTCTGGTGCT
GGTCCTGCTGGGCCCTATGCCAAGGAGTCTGGGATCTGGGCTTACTACGAGATCTGTACC
TTCCTGAAAAATGGAGCCACTCAGGGATGGGATGCCCCTCAGGAAGTGCCTTATGCCTAT
CAGGGCAATGTGTGGGTTGGCTATGACAACGTCAAGAGCTTCGATATTAAGGCTCAATGG
CTTAAGCACAACAAATTTGGAGGCGCCATGGTCTGGGCCATTGATCTGGATGACTTCACT
GGCACTTTCTGCAACCAGGGCAAGTTTCCCCTAATCTCCACCCTGAAGAAGGCCCTTGGC
CTGCAGAGTGCAAGTTGCACGGCTCCAGCTCAGCCCATTGAGCCAATAACTGCTGCTCCC
AGTGGCAGCGGGAACGGGAGCGGGAGTAGCAGCTCTGGAGGCAGCTCGGGAGGCAGTGGA
TTCTGTGCTGGCAGAGCCAACGGCCTCTACCCCGTGGCAAATAACAGAAATGCCTTCTGG
CACTGCGTGAATGGAGTCACGTACCAGCAGAACTGCCAGGCCGGGCTTGTCTTCGACACC
AGCTGTGATTGCTGCAACTGGGCATAA
|
| Enzyme 2 GenBank Gene ID |
AB025008  |
| Enzyme 2 GeneCard ID |
CHIA  |
| Enzyme 2 GenAtlas ID |
CHIA  |
| Enzyme 2 HGNC ID |
HGNC:17432  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p13.1-p21.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Saito A, Ozaki K, Fujiwara T, Nakamura Y, Tanigami A: Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member. Gene. 1999 Nov 1;239(2):325-31. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6319 |
| Enzyme 3 Name |
Chitotriosidase-1 precursor |
| Enzyme 3 Synonyms |
- Chitinase-1
|
| Enzyme 3 Gene Name |
CHIT1 |
| Enzyme 3 Protein Sequence |
>Chitotriosidase-1 precursor
MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAG
MTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFV
NSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLL
SAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAAS
LNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGM
LAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWAL
DLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFC
QGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN
|
| Enzyme 3 Number of Residues |
466 |
| Enzyme 3 Molecular Weight |
51682 |
| Enzyme 3 Theoretical pI |
6.96 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Degrades chitin and chitotriose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- Random hydrolysis of N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin and chitodextrins
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1050958  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q13231  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CHIT1_HUMAN  |
| Enzyme 3 PDB ID |
1WB0  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1401 bp
ATGGTGCGGTCTGTGGCCTGGGCAGGTTTCATGGTCCTGCTGATGATCCCATGGGGCTCT
GCTGCAAAACTGGTCTGCTACTTCACCAACTGGGCCCAGTACAGACAGGGGGAGGCTCGC
TTCCTGCCCAAGGACTTGGACCCCAGCCTTTGCACCCACCTCATCTACGCCTTCGCTGGC
ATGACCAACCACCAGCTGAGCACCACTGAGTGGAATGACGAGACTCTCTACCAGGAGTTC
AATGGCCTGAAGAAGATGAATCCCAAGCTGAAGACCCTGTTAGCCATCGGAGGCTGGAAT
TTCGGCACTCAGAAGTTCACAGATATGGTAGCCACGGCCAACAACCGTCAGACCTTTGTC
AACTCGGCCATCAGGTTTCTGCGCAAATACAGCTTTGACGGCCTTGACCTTGACTGGGAG
TACCCAGGAAGCCAGGGGAGCCCTGCCGTAGACAAGGAGCGCTTCACAACCCTGGTACAG
GACTTGGCCAATGCCTTCCAGCAGGAAGCCCAGACCTCAGGGAAGGAACGCCTTCTTCTG
AGTGCAGCGGTTCCAGCTGGGCAGACCTATGTGGATGCTGGATACGAGGTGGACAAAATC
GCCCAGAACCTGGATTTTGTCAACCTTATGGCCTACGACTTCCATGGCTCTTGGGAGAAG
GTCACGGGACATAACAGCCCCCTCTACAAGAGGCAAGAAGAGAGTGGTGCAGCAGCCAGC
CTCAACGTGGATGCTGCTGTGCAACAGTGGCTGCAGAAGGGGACCCCTGCCAGCAAGCTG
ATCCTTGGCATGCCTACCTACGGACGCTCCTTCACACTGGCCTCCTCATCAGACACCAGA
GTGGGGGCCCCAGCCACAGGGTCTGGCACTCCAGGCCCCTTCACCAAGGAAGGAGGGATG
CTGGCCTACTATGAAGTCTGCTCCTGGAAGGGGGCCACCAAACAGAGAATCCAGGATCAG
AAGGTGCCCTACATCTTCCGGGACAACCAGTGGGTGGGCTTTGATGATGTGGAGAGCTTC
AAAACCAAGGTCAGCTATCTGAAGCAGAAGGGACTGGGCGGGGCCATGGTCTGGGCACTG
GACTTAGATGACTTTGCCGGCTTCTCCTGCAACCAGGGCCGATACCCCCTCATCCAGACG
CTACGGCAGGAACTGAGTCTTCCATACTTGCCTTCAGGCACCCCAGAGCTTGAAGTTCCA
AAACCAGGTCAGCCCTCTGAACCTGAGCATGGCCCCAGCCCTGGACAAGACACGTTCTGC
CAGGGCAAAGCTGATGGGCTCTATCCCAATCCTCGGGAACGGTCCAGCTTCTACAGCTGT
GCAGCGGGGCGGCTGTTCCAGCAAAGCTGCCCGACAGGCCTGGTGTTCAGCAACTCCTGC
AAATGCTGCACCTGGAATTGA
|
| Enzyme 3 GenBank Gene ID |
U29615  |
| Enzyme 3 GeneCard ID |
CHIT1  |
| Enzyme 3 GenAtlas ID |
CHIT1  |
| Enzyme 3 HGNC ID |
HGNC:1936  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1q31-q32 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Boot RG, Renkema GH, Strijland A, van Zonneveld AJ, Aerts JM: Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J Biol Chem. 1995 Nov 3;270(44):26252-6. [PubMed
]
- Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM: Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J Biol Chem. 1995 Feb 3;270(5):2198-202. [PubMed
]
- Boot RG, Renkema GH, Verhoek M, Strijland A, Bliek J, de Meulemeester TM, Mannens MM, Aerts JM: The human chitotriosidase gene. Nature of inherited enzyme deficiency. J Biol Chem. 1998 Oct 2;273(40):25680-5. [PubMed
]
- Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM: Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J Biol Chem. 2002 Jul 12;277(28):25537-44. Epub 2002 Apr 17. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
16921 |
| Enzyme 4 Name |
Chitinase family protein 3 |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
Not Available |
| Enzyme 4 Protein Sequence |
>Chitinase family protein 3
ETSSSVHEQVADSGAQAVAFQSGGESSIVWSCPYTEFAARNSQLKTLLAIGGWNFGTAPF
TAMVSTPENRQTFITSVIRFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAF
EQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENS
PLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTS
GAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKA
QWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITA
APSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVF
DTSCDCCNWA
|
| Enzyme 4 Number of Residues |
430 |
| Enzyme 4 Molecular Weight |
46616 |
| Enzyme 4 Theoretical pI |
4.81 |
| Enzyme 4 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q2VT96  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
Q2VT96_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AY825504  |
| Enzyme 4 GeneCard ID |
Q2VT96  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
HGNC:17432  |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
Not Available |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
16922 |
| Enzyme 5 Name |
Chitinase family protein V2 |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
Not Available |
| Enzyme 5 Protein Sequence |
>Chitinase family protein V2
MREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGY
TGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGI
GAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNVKS
FDIKAQWLKHNKSGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPI
EPITAAPSGSGNGSGSSSSGGSSGGSGFCAGRANGLYPVASNRNAFWHCVNGVTYQQNCQ
AGLVFDTSCDCCNWA
|
| Enzyme 5 Number of Residues |
315 |
| Enzyme 5 Molecular Weight |
33763 |
| Enzyme 5 Theoretical pI |
5.26 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q1M0P3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q1M0P3_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AY911311  |
| Enzyme 5 GeneCard ID |
Q1M0P3  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
HGNC:17432  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
Not Available |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
16923 |
| Enzyme 6 Name |
Chitinase family protein V1 |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
Not Available |
| Enzyme 6 Protein Sequence |
>Chitinase family protein V1
MREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYVHVMTYDLHGSWEGY
TGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGI
GAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWAGYDNVKS
FDIKAQWLKHNKSGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPI
EPITAAPSGSGNGSGSSSSGGSSGGSGFCAGRANGLYPVANNRNAFWHCVNGVTYQQNCQ
AGLVFDTSCDCCNWA
|
| Enzyme 6 Number of Residues |
315 |
| Enzyme 6 Molecular Weight |
33748 |
| Enzyme 6 Theoretical pI |
5.26 |
| Enzyme 6 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q1M0P4  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q1M0P4_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AY911310  |
| Enzyme 6 GeneCard ID |
Q1M0P4  |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
HGNC:17432  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
Not Available |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
17158 |
| Enzyme 7 Name |
cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
Not Available |
| Enzyme 7 Protein Sequence |
>cDNA FLJ76132, highly similar to Homo sapiens chitinase, acidic (CHIA), mRNA
MVSTPENRQTSITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQ
EAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPL
YKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGA
GPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQW
LKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAP
SGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDT
SCDCCNWA
|
| Enzyme 7 Number of Residues |
368 |
| Enzyme 7 Molecular Weight |
40079 |
| Enzyme 7 Theoretical pI |
4.97 |
| Enzyme 7 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
A8K3T7  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
A8K3T7_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
AK290702  |
| Enzyme 7 GeneCard ID |
A8K3T7  |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
Not Available |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
17159 |
| Enzyme 8 Name |
CHIA protein |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
CHIA |
| Enzyme 8 Protein Sequence |
>CHIA protein
KAYSPHRSCPYTEFAARNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIRFLRQ
YEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGIS
NIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNY
WKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTF
LKNGATQGWDAPQEVPYAYQGNVWVGYDNVKSFDIKAQWLKHNKSGGAMVWAIDLDDFTG
TFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGF
CAGRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
|
| Enzyme 8 Number of Residues |
407 |
| Enzyme 8 Molecular Weight |
44307 |
| Enzyme 8 Theoretical pI |
5.90 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
A5D6V7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
A5D6V7_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
BC139901  |
| Enzyme 8 GeneCard ID |
A5D6V7  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
17160 |
| Enzyme 9 Name |
Chitinase, acidic |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
CHIA |
| Enzyme 9 Protein Sequence |
>Chitinase, acidic
YSPHRSCPYTEFAARNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYE
FDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNI
QSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWK
DNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLK
NGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTF
CNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCA
VRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
|
| Enzyme 9 Number of Residues |
405 |
| Enzyme 9 Molecular Weight |
44195 |
| Enzyme 9 Theoretical pI |
5.61 |
| Enzyme 9 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q5VUV3  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
Q5VUV3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
AL513202  |
| Enzyme 9 GeneCard ID |
Q5VUV3  |
| Enzyme 9 GenAtlas ID |
CHIA  |
| Enzyme 9 HGNC ID |
HGNC:17432  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
17161 |
| Enzyme 10 Name |
Chitinase, acidic |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
CHIA |
| Enzyme 10 Protein Sequence |
>Chitinase, acidic
ETSSSVHEQVADSGAQAVAFQSGGESSIVWNSQLKTLLAIGGWNFGTAPFTAMVSTPENR
QTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKP
RLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTG
SNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAK
ESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGG
AMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSG
SSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
|
| Enzyme 10 Number of Residues |
420 |
| Enzyme 10 Molecular Weight |
45462 |
| Enzyme 10 Theoretical pI |
4.79 |
| Enzyme 10 GO Classification |
| Function |
- binding
- catalytic activity
- chitin binding
- chitinase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- pattern binding
- polysaccharide binding
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- carbohydrate metabolism
- chitin catabolism
- chitin metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
|
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q5VUV5  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
Q5VUV5_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
Not Available |
| Enzyme 10 GenBank Gene ID |
AL513202  |
| Enzyme 10 GeneCard ID |
Q5VUV5  |
| Enzyme 10 GenAtlas ID |
CHIA  |
| Enzyme 10 HGNC ID |
HGNC:17432  |
| Enzyme 10 Chromosome Location |
Not Available |
| Enzyme 10 Locus |
Not Available |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |