We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for D-Serine (HMDB03406)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 21:15:26
Update Date 2010-01-19 13:05:09
Accession Number HMDB03406
Secondary Accession Numbers Not Available
Common Name D-Serine
Description A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from glycine or threonine. It is involved in the biosynthesis of purines, pyrimidines, and other amino acids. As a constituent (residue) of proteins, its side chain can undergo O-linked glycosylation. This might be important in explaining some of the devastating consequences of diabetes. It is one of three amino acid residues that are commonly phosphorylated by kinases during cell signalling in eukaryotes. Phosphorylated serine residues are often referred to as phosphoserine. Serine proteases are a common type of protease. Serine (IPA [sejin]), organic compound, one of the 20 amino acids commonly found in animal proteins. Only the L-stereoisomer appears in mammalian protein. It is not essential to the human diet, since it can be synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865. Its name is derived from the Latin for silk, sericum. Serine's structure was established in 1902.
Synonyms
  1. (2R)-2-amino-3-hydroxypropanoate
  2. (2R)-2-amino-3-hydroxypropanoic acid
  3. (R)-2-amino-3-hydroxypropanoate
  4. (R)-2-amino-3-hydroxypropanoic acid
  5. D-Serin
  6. DL-Serine
  7. DSN
  8. Serine D-form
Chemical IUPAC Name (2R)-2-amino-3-hydroxy-propanoic acid
Chemical Formula C3H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • 1,2-aminoalcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Component of Glycine, serine and threonine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 105.093
Monoisotopic Molecular Weight 105.042595
Isomeric SMILES N[C@H](CO)C(O)=O
Canonical SMILES NC(CO)C(O)=O
KEGG Compound ID C00740 Link Image
BioCyc ID Serines Link Image
BiGG ID 35846 Link Image
Wikipedia Link DSN Link Image
NuGOwiki Link HMDB03406 Link Image
Metagene Link HMDB03406 Link Image
METLIN ID 6920 Link Image
PubChem Compound 71077 Link Image
PubChem Substance 839068 Link Image
ChEBI ID 16523 Link Image
CAS Registry Number 312-84-5
InChI Identifier InChI=1/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m1/s1
Synthesis Reference Zhu, Yanxin; Yuan, Minglong; Yuan, Mingwei; Du, Bilin; Zheng, Ling. Preparation of D-serine from acetylglycine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2006), 4pp.
Melting Point (Experimental) 229 oC
Experimental Water Solubility 364 mg/mL at 20 oC [BEILSTEIN] Source: PhysProp
Predicted Water Solubility 480.00003 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.42 [Predicted by ALOGPS]; -4 [Predicted by PubChem via XLOGP]; -3.46 [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 Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Adipose Tissue —
Epidermis —
Fibroblasts —
Intestine —
Kidney —
Lung —
Muscle —
Myelin —
Neuron —
Pancreas —
Placenta —
Platelet —
Prostate —
Skeletal Muscle —
Spleen —
Stratum Corneum —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 3.6 +/- 2.2 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Grant SL, Shulman Y, Tibbo P, Hampson DR, Baker GB: Determination of d-serine and related neuroactive amino acids in human plasma by high-performance liquid chromatography with fluorimetric detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Dec 5;844(2):278-82. Epub 2006 Aug 4. [PubMed Link Image]
Biofluid Blood
Value 2.28 +/- 0.59 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hashimoto K, Fukushima T, Shimizu E, Komatsu N, Watanabe H, Shinoda N, Nakazato M, Kumakiri C, Okada S, Hasegawa H, Imai K, Iyo M: Decreased serum levels of D-serine in patients with schizophrenia: evidence in support of the N-methyl-D-aspartate receptor hypofunction hypothesis of schizophrenia. Arch Gen Psychiatry. 2003 Jun;60(6):572-6. [PubMed Link Image]
Biofluid CSF
Value 52.0 (25.0-105.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jones CM, Smith M, Henderson MJ: Reference data for cerebrospinal fluid and the utility of amino acid measurement for the diagnosis of inborn errors of metabolism. Ann Clin Biochem. 2006 Jan;43(Pt 1):63-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 1.86 +/- 0.53 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Hashimoto K, Fukushima T, Shimizu E, Komatsu N, Watanabe H, Shinoda N, Nakazato M, Kumakiri C, Okada S, Hasegawa H, Imai K, Iyo M: Decreased serum levels of D-serine in patients with schizophrenia: evidence in support of the N-methyl-D-aspartate receptor hypofunction hypothesis of schizophrenia. Arch Gen Psychiatry. 2003 Jun;60(6):572-6. [PubMed Link Image]
Associated Disorders
Condition References
Schizophrenia
  • Hashimoto K, Fukushima T, Shimizu E, Komatsu N, Watanabe H, Shinoda N, Nakazato M, Kumakiri C, Okada S, Hasegawa H, Imai K, Iyo M: Decreased serum levels of D-serine in patients with schizophrenia: evidence in support of the N-methyl-D-aspartate receptor hypofunction hypothesis of schizophrenia. Arch Gen Psychiatry. 2003 Jun;60(6):572-6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Hansson L, Stromqvist M, Backman A, Wallbrandt P, Carlstein A, Egelrud T: Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase. J Biol Chem. 1994 Jul 29;269(30):19420-6. [PubMed Link Image]
  2. Jones CM, Smith M, Henderson MJ: Reference data for cerebrospinal fluid and the utility of amino acid measurement for the diagnosis of inborn errors of metabolism. Ann Clin Biochem. 2006 Jan;43(Pt 1):63-6. [PubMed Link Image]
  3. Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed Link Image]
  4. Deshpande RV, Goust JM, Hogan EL, Banik NL: Calpain secreted by activated human lymphoid cells degrades myelin. J Neurosci Res. 1995 Oct 1;42(2):259-65. [PubMed Link Image]
  5. Metzner L, Kottra G, Neubert K, Daniel H, Brandsch M: Serotonin, L-tryptophan, and tryptamine are effective inhibitors of the amino acid transport system PAT1. FASEB J. 2005 Sep;19(11):1468-73. [PubMed Link Image]
  6. Nagata Y, Higashi M, Ishii Y, Sano H, Tanigawa M, Nagata K, Noguchi K, Urade M: The presence of high concentrations of free D-amino acids in human saliva. Life Sci. 2006 Mar 6;78(15):1677-81. Epub 2006 Feb 9. [PubMed Link Image]
  7. Nuesch JP, Corbau R, Tattersall P, Rommelaere J: Biochemical activities of minute virus of mice nonstructural protein NS1 are modulated In vitro by the phosphorylation state of the polypeptide. J Virol. 1998 Oct;72(10):8002-12. [PubMed Link Image]
  8. Tsuei DJ, Hsu HC, Lee PH, Jeng YM, Pu YS, Chen CN, Lee YC, Chou WC, Chang CJ, Ni YH, Chang MH: RBMY, a male germ cell-specific RNA-binding protein, activated in human liver cancers and transforms rodent fibroblasts. Oncogene. 2004 Jul 29;23(34):5815-22. [PubMed Link Image]
  9. Yu LY, Jokitalo E, Sun YF, Mehlen P, Lindholm D, Saarma M, Arumae U: GDNF-deprived sympathetic neurons die via a novel nonmitochondrial pathway. J Cell Biol. 2003 Dec 8;163(5):987-97. Epub 2003 Dec 1. [PubMed Link Image]
  10. Franzke CW, Baici A, Bartels J, Christophers E, Wiedow O: Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation. J Biol Chem. 1996 Sep 6;271(36):21886-90. [PubMed Link Image]
  11. Hooper JD, Nicol DL, Dickinson JL, Eyre HJ, Scarman AL, Normyle JF, Stuttgen MA, Douglas ML, Loveland KA, Sutherland GR, Antalis TM: Testisin, a new human serine proteinase expressed by premeiotic testicular germ cells and lost in testicular germ cell tumors. Cancer Res. 1999 Jul 1;59(13):3199-205. [PubMed Link Image]
  12. Ishida-Takahashi R, Rosario F, Gong Y, Kopp K, Stancheva Z, Chen X, Feener EP, Myers MG Jr: Phosphorylation of Jak2 on Ser(523) inhibits Jak2-dependent leptin receptor signaling. Mol Cell Biol. 2006 Jun;26(11):4063-73. [PubMed Link Image]
  13. Farhana L, Dawson MI, Huang Y, Zhang Y, Rishi AK, Reddy KB, Freeman RS, Fontana JA: Apoptosis signaling by the novel compound 3-Cl-AHPC involves increased EGFR proteolysis and accompanying decreased phosphatidylinositol 3-kinase and AKT kinase activities. Oncogene. 2004 Mar 11;23(10):1874-84. [PubMed Link Image]
  14. Taniguchi A, Kataoka K, Kono T, Oseko F, Okuda H, Nagata I, Imura H: Parathyroid hormone-induced lipolysis in human adipose tissue. J Lipid Res. 1987 May;28(5):490-4. [PubMed Link Image]
  15. Dietze-Schroeder D, Sell H, Uhlig M, Koenen M, Eckel J: Autocrine action of adiponectin on human fat cells prevents the release of insulin resistance-inducing factors. Diabetes. 2005 Jul;54(7):2003-11. [PubMed Link Image]
  16. Nanda N, Bao M, Lin H, Clauser K, Komuves L, Quertermous T, Conley PB, Phillips DR, Hart MJ: Platelet endothelial aggregation receptor 1 (PEAR1), a novel epidermal growth factor repeat-containing transmembrane receptor, participates in platelet contact-induced activation. J Biol Chem. 2005 Jul 1;280(26):24680-9. Epub 2005 Apr 25. [PubMed Link Image]
  17. Stewart LV, Song K, Hsing AY, Danielpour D: Regulation of trespin expression by modulators of cell growth, differentiation, and apoptosis in prostatic epithelial cells. Exp Cell Res. 2003 Apr 1;284(2):303-15. [PubMed Link Image]
  18. Pfundt R, van Ruissen F, van Vlijmen-Willems IM, Alkemade HA, Zeeuwen PL, Jap PH, Dijkman H, Fransen J, Croes H, van Erp PE, Schalkwijk J: Constitutive and inducible expression of SKALP/elafin provides anti-elastase defense in human epithelia. J Clin Invest. 1996 Sep 15;98(6):1389-99. [PubMed Link Image]
  19. Strauss JF 3rd, Kallen CB, Christenson LK, Watari H, Devoto L, Arakane F, Kiriakidou M, Sugawara T: The steroidogenic acute regulatory protein (StAR): a window into the complexities of intracellular cholesterol trafficking. Recent Prog Horm Res. 1999;54:369-94; discussion 394-5. [PubMed Link Image]
  20. Kim JK, Fillmore JJ, Sunshine MJ, Albrecht B, Higashimori T, Kim DW, Liu ZX, Soos TJ, Cline GW, O'Brien WR, Littman DR, Shulman GI: PKC-theta knockout mice are protected from fat-induced insulin resistance. J Clin Invest. 2004 Sep;114(6):823-7. [PubMed Link Image]
  21. Olive PL, Banath JP, Sinnott LT: Phosphorylated histone H2AX in spheroids, tumors, and tissues of mice exposed to etoposide and 3-amino-1,2,4-benzotriazine-1,3-dioxide. Cancer Res. 2004 Aug 1;64(15):5363-9. [PubMed Link Image]
  22. Hinek A, Smith AC, Cutiongco EM, Callahan JW, Gripp KW, Weksberg R: Decreased elastin deposition and high proliferation of fibroblasts from Costello syndrome are related to functional deficiency in the 67-kD elastin-binding protein. Am J Hum Genet. 2000 Mar;66(3):859-72. [PubMed Link Image]
  23. Lavker RM, Risse B, Brown H, Ginsburg D, Pearson J, Baker MS, Jensen PJ: Localization of plasminogen activator inhibitor type 2 (PAI-2) in hair and nail: implications for terminal differentiation. J Invest Dermatol. 1998 Jun;110(6):917-22. [PubMed Link Image]
  24. Paju A, Bjartell A, Zhang WM, Nordling S, Borgstrom A, Hansson J, Stenman UH: Expression and characterization of trypsinogen produced in the human male genital tract. Am J Pathol. 2000 Dec;157(6):2011-21. [PubMed Link Image]
  25. Schultess J, Danielewski O, Smolenski AP: Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets. Blood. 2005 Apr 15;105(8):3185-92. Epub 2005 Jan 4. [PubMed Link Image]
  26. Alvarez JV, Greulich H, Sellers WR, Meyerson M, Frank DA: Signal transducer and activator of transcription 3 is required for the oncogenic effects of non-small-cell lung cancer-associated mutations of the epidermal growth factor receptor. Cancer Res. 2006 Mar 15;66(6):3162-8. [PubMed Link Image]
  27. Hayes GM, Carrigan PE, Beck AM, Miller LJ: Targeting the RNA splicing machinery as a novel treatment strategy for pancreatic carcinoma. Cancer Res. 2006 Apr 1;66(7):3819-27. [PubMed Link Image]
  28. Roesch PL, Redford P, Batchelet S, Moritz RL, Pellett S, Haugen BJ, Blattner FR, Welch RA: Uropathogenic Escherichia coli use d-serine deaminase to modulate infection of the murine urinary tract. Mol Microbiol. 2003 Jul;49(1):55-67. [PubMed Link Image]
  29. Amberger VR, Hensel T, Ogata N, Schwab ME: Spreading and migration of human glioma and rat C6 cells on central nervous system myelin in vitro is correlated with tumor malignancy and involves a metalloproteolytic activity. Cancer Res. 1998 Jan 1;58(1):149-58. [PubMed Link Image]
  30. Wyatt AW, Hussain A, Amann K, Klingel K, Kandolf R, Artunc F, Grahammer F, Huang DY, Vallon V, Kuhl D, Lang F: DOCA-induced phosphorylation of glycogen synthase kinase 3beta. Cell Physiol Biochem. 2006;17(3-4):137-44. Epub 2006 Mar 14. [PubMed Link Image]
  31. Khamzina L, Veilleux A, Bergeron S, Marette A: Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance. Endocrinology. 2005 Mar;146(3):1473-81. Epub 2004 Dec 16. [PubMed Link Image]
  32. Morino K, Petersen KF, Dufour S, Befroy D, Frattini J, Shatzkes N, Neschen S, White MF, Bilz S, Sono S, Pypaert M, Shulman GI: Reduced mitochondrial density and increased IRS-1 serine phosphorylation in muscle of insulin-resistant offspring of type 2 diabetic parents. J Clin Invest. 2005 Dec;115(12):3587-93. Epub 2005 Nov 10. [PubMed Link Image]
  33. Zhu L, Wigle D, Hinek A, Kobayashi J, Ye C, Zuker M, Dodo H, Keeley FW, Rabinovitch M: The endogenous vascular elastase that governs development and progression of monocrotaline-induced pulmonary hypertension in rats is a novel enzyme related to the serine proteinase adipsin. J Clin Invest. 1994 Sep;94(3):1163-71. [PubMed Link Image]
  34. Boehning D, Snyder SH: Novel neural modulators. Annu Rev Neurosci. 2003;26:105-31. [PubMed Link Image]
  35. Wikipedia Link Image
Metabolic Enzymes
  1. Asc-type amino acid transporter 1
  2. Serine racemase
  3. cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 8479
Enzyme 1 Name Asc-type amino acid transporter 1
Enzyme 1 Synonyms
  1. Asc-1
Enzyme 1 Gene Name SLC7A10
Enzyme 1 Protein Sequence >Asc-type amino acid transporter 1 
MAGHTQQPSGRGNPRPAPSPSPVPGTVPGASERVALKKEIGLLSACTIIIGNIIGSGIFI
SPKGVLEHSGSVGLALFVWVLGGGVTALGSLCYAELGVAIPKSGGDYAYVTEIFGGLAGF
LLLWSAVLIMYPTSLAVISMTFSNYVLQPVFPNCIPPTTASRVLSMACLMLLTWVNSSSV
RWATRIQDMFTGGKLLALSLIIGVGLLQIFQGHFEELRPSNAFAFWMTPSVGHLALAFLQ
GSFAFSGWNFLNYVTEEMVDARKNLPRAIFISIPLVTFVYTFTNIAYFTAMSPQELLSSN
AVAVTFGEKLLGYFSWVMPVSVALSTFGGINGYLFTYSRLCFSGAREGHLPSLLAMIHVR
HCTPIPALLVCCGATAVIMLVGDTYTLINYVSFINYLCYGVTILGLLLLRWRRPALHRPI
KVNLLIPVAYLVFWAFLLVFSFISEPMVCGVGVIIILTGVPIFFLGVFWRSKPKCVHRLT
ESMTHWGQELCFVVYPQDAPEEEENGPCPPSLLPATDKPSKPQ
Enzyme 1 Number of Residues 523
Enzyme 1 Molecular Weight 56799
Enzyme 1 Theoretical pI 8.24
Enzyme 1 GO Classification
Function
  • amine transporter activity
  • amino acid transporter activity
  • amino acid-polyamine transporter activity
  • transporter activity
Process
  • amine transport
  • amino acid transport
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Sodium-independent, high affinity transport of small neutral D- and L-amino acids. May play a role in the modulation of glutamatergic transmission through mobilization of D-serine at the glutamatergic synapse
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-136
Enzyme 1 Transmembrane Regions
  • 40-60 72-92 113-133 268-288 310-330 362-382 388-408 424-444 448-468
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 9309293 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NS82 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AAA1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1572 bp 
ATGGCCGGCCACACGCAGCAGCCGAGCGGGCGCGGGAACCCCAGGCCTGCGCCCTCGCCC
TCCCCAGTCCCAGGGACCGTCCCCGGCGCCTCGGAGCGGGTGGCGCTCAAGAAGGAGATC
GGGCTGCTGAGCGCCTGCACCATCATCATCGGGAACATCATCGGCTCGGGCATCTTCATC
TCGCCCAAGGGGGTCCTGGAGCACTCAGGCTCCGTGGGTCTGGCCCTGTTCGTCTGGGTC
CTGGGTGGGGGCGTGACGGCTCTGGGCTCCCTCTGCTATGCAGAGCTGGGAGTCGCCATC
CCCAAGTCTGGCGGGGACTACGCCTACGTCACAGAGATCTTCGGGGGCCTGGCTGGCTTT
CTGCTGCTCTGGAGCGCCGTCCTCATCATGTACCCCACCAGCCTTGCTGTCATCTCCATG
ACCTTCTCCAACTACGTGCTGCAGCCCGTGTTCCCCAACTGCATCCCCCCCACCACAGCC
TCCCGGGTGCTGTCCATGGCCTGCCTGATGCTCCTGACATGGGTGAACAGCTCCAGTGTG
CGCTGGGCCACGCGCATCCAGGACATGTTCACAGGCGGGAAGCTGCTGGCCTTGTCCCTC
ATCATCGGCGTGGGCCTTCTCCAGATCTTCCAAGGACACTTCGAGGAGCTGAGGCCCAGC
AATGCCTTTGCTTTCTGGATGACGCCCTCCGTGGGACACCTGGCCCTGGCCTTCCTCCAG
GGCTCCTTCGCCTTCAGTGGCTGGAACTTCCTCAACTATGTCACCGAGGAGATGGTTGAC
GCCCGAAAGAACCTACCTCGCGCCATCTTCATCTCCATCCCACTGGTGACCTTCGTGTAC
ACGTTCACCAACATTGCCTACTTCACGGCCATGTCCCCCCAGGAGCTGCTCTCCTCCAAT
GCGGTGGCTGTGACCTTCGGGGAGAAGCTGCTGGGCTACTTTTCTTGGGTCATGCCTGTC
TCCGTGGCTCTGTCAACCTTCGGAGGGATCAATGGTTACCTGTTCACCTACTCCAGGCTG
TGCTTCTCTGGAGCCCGCGAGGGGCACCTGCCCAGCCTGCTGGCCATGATCCACGTCAGA
CACTGCACCCCCATCCCCGCCCTCCTCGTCTGTTGCGGGGCCACAGCCGTCATCATGCTC
GTGGGCGACACGTACACGCTCATCAACTATGTGTCCTTCATCAACTACCTCTGCTACGGC
GTCACCATCCTGGGCCTGCTGCTGCTGCGCTGGAGGCGGCCTGCACTCCACAGGCCCATC
AAGGTGAACCTTCTCATCCCCGTGGCGTACTTGGTCTTCTGGGCCTTCCTGCTGGTCTTC
AGCTTCATCTCAGAGCCTATGGTCTGTGGGGTCGGCGTCATCATCATCCTTACGGGGGTG
CCCATTTTCTTTCTGGGAGTGTTCTGGAGAAGCAAACCAAAGTGTGTGCACAGACTCACA
GAGTCCATGACACACTGGGGCCAGGAGCTGTGTTTCGTGGTCTACCCCCAGGACGCCCCC
GAAGAGGAGGAGAATGGCCCCTGCCCACCCTCCCTGCTGCCTGCCACAGACAAGCCCTCG
AAGCCACAATGA
Enzyme 1 GenBank Gene ID AB037670 Link Image
Enzyme 1 GeneCard ID SLC7A10 Link Image
Enzyme 1 GenAtlas ID SLC7A10 Link Image
Enzyme 1 HGNC ID HGNC:11058 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19q13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Nakauchi J, Matsuo H, Kim DK, Goto A, Chairoungdua A, Cha SH, Inatomi J, Shiokawa Y, Yamaguchi K, Saito I, Endou H, Kanai Y: Cloning and characterization of a human brain Na(+)-independent transporter for small neutral amino acids that transports D-serine with high affinity. Neurosci Lett. 2000 Jun 30;287(3):231-5. [PubMed Link Image]
  2. Leclerc D, Wu Q, Ellis JR, Goodyer P, Rozen R: Is the SLC7A10 gene on chromosome 19 a candidate locus for cystinuria? Mol Genet Metab. 2001 Aug;73(4):333-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 14709
Enzyme 2 Name Serine racemase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name SRR
Enzyme 2 Protein Sequence >Serine racemase 
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGA
LNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQA
YGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDAL
VVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGV
KSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQT
VSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
Enzyme 2 Number of Residues 340
Enzyme 2 Molecular Weight 36567
Enzyme 2 Theoretical pI 6.51
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Catalyzes the synthesis of D-serine from L-serine
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 11034785 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9GZT4 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SRR_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1023 bp 
ATGTGTGCTCAGTATTGCATCTCCTTTGCTGATGTTGAAAAAGCTCATATCAACATTCGA
GATTCTATCCACCTCACACCAGTGCTAACAAGCTCCATTTTGAATCAACTAACAGGGCGC
AATCTTTTCTTCAAATGTGAACTCTTCCAGAAAACAGGATCTTTTAAGATTCGTGGTGCT
CTCAATGCCGTCAGAAGCTTGGTTCCTGATGCTTTAGAAAGGAAGCCGAAAGCTGTTGTT
ACTCACAGCAGTGGAAACCATGGCCAGGCTCTCACCTATGCTGCCAAATTGGAAGGAATT
CCTGCTTATATTGTGGTGCCCCAGACAGCTCCAGACTGTAAAAAACTTGCAATACAAGCC
TACGGAGCGTCAATTGTATACTGTGAACCTAGTGATGAGTCCAGAGAAAATGTTGCAAAA
AGAGTTACAGAAGAAACAGAAGGCATCATGGTACATCCCAACCAGGAGCCTGCAGTGATA
GCTGGACAAGGGACAATTGCCCTGGAAGTGCTGAACCAGGTTCCTTTGGTGGATGCACTG
GTGGTACCTGTAGGTGGAGGAGGAATGCTTGCTGGAATAGCAATTACAGTTAAGGCTCTG
AAACCTAGTGTGAAGGTATATGCTGCTGAACCCTCAAATGCAGATGACTGCTACCAGTCC
AAGCTGAAGGGGAAACTGATGCCCAATCTTTATCCTCCAGAAACCATAGCAGATGGTGTC
AAATCCAGCATTGGCTTGAACACCTGGCCTATTATCAGGGACCTTGTGGATGATATCTTC
ACTGTCACAGAGGATGAAATTAAGTGTGCAACCCAGCTGGTGTGGGAGAGGATGAAACTA
CTCATTGAACCTACAGCTGGTGTTGGAGTGGCTGCTGTGCTGTCTCAACATTTTCAAACT
GTTTCCCCAGAAGTAAAGAACATTTGTATTGTGCTCAGTGGTGGAAATGTAGACTTAACC
TCCTCCATAACTTGGGTGAAGCAGGCTGAAAGGCCAGCTTCTTATCAGTCTGTTTCTGTT
TAA
Enzyme 2 GenBank Gene ID AF169974 Link Image
Enzyme 2 GeneCard ID Q9GZT4 Link Image
Enzyme 2 GenAtlas ID SRR Link Image
Enzyme 2 HGNC ID HGNC:14398 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. De Miranda J, Santoro A, Engelender S, Wolosker H: Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 16507
Enzyme 3 Name cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name PSPH
Enzyme 3 Protein Sequence >cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a) 
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
Enzyme 3 Number of Residues 225
Enzyme 3 Molecular Weight 25008
Enzyme 3 Theoretical pI 5.42
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • phosphoserine phosphatase activity
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B2RCR5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B2RCR5_HUMAN Link Image
Enzyme 3 PDB ID 1NNL Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK315235 Link Image
Enzyme 3 GeneCard ID B2RCR5 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available