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Human Metabolome Database Version 2.5

 

Showing metabocard for Biliverdin (HMDB01008)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:28
Accession Number HMDB01008
Secondary Accession Numbers HMDB02309
Common Name Biliverdin
Description Biliverdin is a green pigment formed as a byproduct of hemoglobin breakdown. It consists of four linearly connected pyrrole rings (a tetrapyrrole). Biliverdin is formed when the heme group in hemoglobin is cleaved at its alpha-methene bridge. The resulting biliverdin is then reduced to bilirubin, a yellow pigment, by the enzyme biliverdin reductase. The changing color of a bruise from deep purple to yellow over time is a graphical indicator of this reaction. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of amphibia and of birds, but not in normal human bile or serum.
Synonyms
  1. 1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone
  2. Biliverdin IX
  3. Biliverdin IX alpha
  4. Biliverdine
  5. Dehydrobilirubin
  6. Protobiliverdin IX
  7. Uteroverdine
Chemical IUPAC Name 3-[2-[(E)-[(5E)-3-(2-carboxyethyl)-5-[(4-ethenyl-3-methyl-5-oxo-pyrrol-2-yl)methylidene]-4-methyl-pyrrol-2-ylidene]methyl]-5-[(E)-(3-ethenyl-4-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-3-yl]propanoic acid
Chemical Formula C33H34N4O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Bilirubins
Family
  • Mammalian Metabolite
Species
  • imine
  • enamine
  • carboxylic acid
  • oxo(het)arene
  • alkene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Porphyrin and chlorophyll metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 582.646
Monoisotopic Molecular Weight 582.247864
Isomeric SMILES CC1=C(C=C)C(NC1=O)=CC1=C(C)C(CCC(O)=O)=C(N1)C=C1NC(=CC2=NC(=O)C(C=C)=C2C)C(C)=C/1CCC(O)=O
Canonical SMILES CC1=C(C=C)C(NC1=O)=CC1=C(C)C(CCC(O)=O)=C(N1)C=C1NC(=CC2=NC(=O)C(C=C)=C2C)C(C)=C1CCC(O)=O
KEGG Compound ID C00500 Link Image
BioCyc ID BILIVERDINE Link Image
BiGG ID 35167 Link Image
Wikipedia Link Biliverdin Link Image
NuGOwiki Link HMDB01008 Link Image
Metagene Link HMDB01008 Link Image
METLIN ID 5938 Link Image
PubChem Compound 5280353 Link Image
PubChem Substance 151372 Link Image
ChEBI ID 17033 Link Image
CAS Registry Number 114-25-0
InChI Identifier InChI=1/C33H34N4O6/c1-7-20-19(6)32(42)37-27(20)14-25-18(5)23(10-12-31(40)41)29(35-25)15-28-22(9-11-30(38)39)17(4)24(34-28)13-26-16(3)21(8-2)33(43)36-26/h7-8,13-15,34-35H,1-2,9-12H2,3-6H3,(H,37,42)(H,38,39)(H,40,41)/b24-13+,27-14-,28-15-
Synthesis Reference Mora, Maria E.; Bari, Sara E.; Awruch, Josefina; Delfino, Jose M. On how the conformation of biliverdins influences their reduction to bilirubins: A biological and molecular modeling study. Bioorganic & Medicinal Chemistry (2003), 11(21), 4661-467
Melting Point (Experimental) >300 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.8e-06 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 0.0123000005 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.77 [Predicted by ALOGPS]; 1.754 [Predicted by PubChem via XLOGP]; 5.04 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
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
  • nucleus
  • Membrane (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Most Tissues —
Neuron —
Placenta —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Briz O, Macias RI, Serrano MA, Gonzalez-Gallego J, Bayon JE, Marin JJ: Excretion of foetal bilirubin by the rat placenta-maternal liver tandem. Placenta. 2003 May;24(5):462-72. [PubMed Link Image]
  2. Trull FR, Ibars O, Lightner DA: Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: evidence from circular dichroism. Arch Biochem Biophys. 1992 Nov 1;298(2):710-4. [PubMed Link Image]
  3. Kunikata T, Itoh S, Ozaki T, Kondo M, Isobe K, Onishi S: Formation of propentdyopents and biliverdin, oxidized metabolites of bilirubin, in infants receiving oxygen therapy. Pediatr Int. 2000 Aug;42(4):331-6. [PubMed Link Image]
  4. Odrcich MJ, Graham CH, Kimura KA, McLaughlin BE, Marks GS, Nakatsu K, Brien JF: Heme oxygenase and nitric oxide synthase in the placenta of the guinea-pig during gestation. Placenta. 1998 Sep;19(7):509-16. [PubMed Link Image]
  5. Poon HF, Calabrese V, Scapagnini G, Butterfield DA: Free radicals: key to brain aging and heme oxygenase as a cellular response to oxidative stress. J Gerontol A Biol Sci Med Sci. 2004 May;59(5):478-93. [PubMed Link Image]
  6. Beruter J, Colombo JP, Schlunegger UP: Isolation and identification of the urinary pigment uroerythrin. Eur J Biochem. 1975 Aug 1;56(1):239-44. [PubMed Link Image]
  7. Chrastil J: Spectrophotometric determination of cysteine and cystine in urine. Analyst. 1990 Oct;115(10):1383-4. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Heme oxygenase 2
  2. Heme oxygenase 1
  3. Biliverdin reductase A precursor
  4. Flavin reductase
  5. cDNA FLJ75742, highly similar to Homo sapiens biliverdin reductase A
  6. Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
Enzyme 1 [top]
Enzyme 1 ID 5383
Enzyme 1 Name Heme oxygenase 2
Enzyme 1 Synonyms
  1. HO-2
Enzyme 1 Gene Name HMOX2
Enzyme 1 Protein Sequence >Heme oxygenase 2 
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG
NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN
WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA
GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL
AAGVALAAGLLAWYYM
Enzyme 1 Number of Residues 316
Enzyme 1 Molecular Weight 36033
Enzyme 1 Theoretical pI 5.09
Enzyme 1 GO Classification
Function
  • catalytic activity
  • heme oxygenase (decyclizing) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Process
  • cellular metabolism
  • heme metabolism
  • heme oxidation
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin metabolism
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter
Enzyme 1 Pathways
Enzyme 1 Reactions
  • heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 296-315
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 443771 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30519 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HMOX2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >951 bp 
ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG
GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG
ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC
AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC
CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC
ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC
TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC
ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT
CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA
GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG
CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG
GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC
GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA
GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC
AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG
GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
Enzyme 1 GenBank Gene ID D21243 Link Image
Enzyme 1 GeneCard ID HMOX2 Link Image
Enzyme 1 GenAtlas ID HMOX2 Link Image
Enzyme 1 HGNC ID HGNC:5014 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J Biol Chem. 1995 Mar 17;270(11):6345-50. [PubMed Link Image]
  2. McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. 1992 May 15;295(1):13-20. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5430
Enzyme 2 Name Heme oxygenase 1
Enzyme 2 Synonyms
  1. HO-1
Enzyme 2 Gene Name HMOX1
Enzyme 2 Protein Sequence >Heme oxygenase 1 
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA
LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE
VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ
LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA
SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Enzyme 2 Number of Residues 288
Enzyme 2 Molecular Weight 32819
Enzyme 2 Theoretical pI 8.68
Enzyme 2 GO Classification
Function
  • catalytic activity
  • heme oxygenase (decyclizing) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Process
  • cellular metabolism
  • heme metabolism
  • heme oxidation
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin metabolism
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed
Enzyme 2 Pathways
Enzyme 2 Reactions
  • heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 265-287
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35173 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09601 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HMOX1_HUMAN Link Image
Enzyme 2 PDB ID 1T5P Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >867 bp 
ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC
ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC
CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC
CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA
GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC
TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG
GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC
CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT
GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG
CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA
GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG
CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC
AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC
ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA
GTTGCTGTAGGGCTTTATGCCATGTGA
Enzyme 2 GenBank Gene ID X06985 Link Image
Enzyme 2 GeneCard ID HMOX1 Link Image
Enzyme 2 GenAtlas ID HMOX1 Link Image
Enzyme 2 HGNC ID HGNC:5013 Link Image
Enzyme 2 Chromosome Location 22
Enzyme 2 Locus 22q12|22q13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S: Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988 Feb 1;171(3):457-61. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Keyse SM, Tyrrell RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989 Jan;86(1):99-103. [PubMed Link Image]
  4. Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem. 1989 Feb 15;179(3):557-63. [PubMed Link Image]
  5. Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL: Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5973
Enzyme 3 Name Biliverdin reductase A precursor
Enzyme 3 Synonyms
  1. Biliverdin-IX alpha- reductase
  2. BVR A
Enzyme 3 Gene Name BLVRA
Enzyme 3 Protein Sequence >Biliverdin reductase A precursor 
MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLE
DALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKV
LHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLF
GELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLEN
VPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
Enzyme 3 Number of Residues 296
Enzyme 3 Molecular Weight 33429
Enzyme 3 Theoretical pI 6.41
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor
Enzyme 3 Pathways
Enzyme 3 Reactions
  • bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1246749 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P53004 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name BIEA_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >891 bp 
ATGAATGCAGAGCCCGAGAGGAAGTTTGGCGTGGTGGTGGTTGGTGTTGGCCGAGCCGGC
TCCGTGCGGATGAGGGACTTGCGGAATCCACACCCTTCCTCAGCGTTCCTGAACCTGATT
GGCTTCGTGTCGAGAAGGGAGCTCGGGAGCATTGATGGAGTCCAGCAGATTTCTTTGGAG
GATGCTCTTTCCAGCCAAGAGGTGGAGGTCGCCTATATCTGCAGTGAGAGCTCCAGCCAT
GAGGACTACATCAGGCAGTTCCTTAATGCTGGCAAGCACGTCCTTGTGGAATACCCCATG
ACACTGTCATTGGCGGCCGCTCAGGAACTGTGGGAGCTGGCTGAGCAGAAAGGAAAAGTC
TTGCACGAGGAGCATGTTGAACTCTTGATGGAGGAATTCGCTTTCCTGAAAAAAGAAGTG
GTGGGGAAAGACCTGCTGAAAGGGTCGCTCCTCTTCACATCTGACCCGTTGGAAGAAGAC
CGGTTTGGCTTCCCTGCATTCAGCGGCATCTCTCGACTGACCTGGCTGGTCTCCCTCTTT
GGGGAGCTTTCTCTTGTGTCTGCCACTTTGGAAGAGCGAAAGGAAGATCAGTATATGAAA
ATGACAGTGTGTCTGGAGACAGAGAAGAAAAGTCCACTGTCATGGATTGAAGAAAAAGGA
CCTGGTCTAAAACGAAACAGATATTTAAGCTTCCATTTCAAGTCTGGGTCCTTGGAGAAT
GTGCCAAATGTAGGAGTGAATAAGAACATATTTCTGAAAGATCAAAATATATTTGTCCAG
AAACTCTTGGGCCAGTTCTCTGAGAAGGAACTGGCTGCTGAAAAGAAACGCATCCTGCAC
TGCCTGGGGCTTGCAGAAGAAATCCAGAAATATTGCTGTTCAAGGAAGTAA
Enzyme 3 GenBank Gene ID X93086 Link Image
Enzyme 3 GeneCard ID BLVRA Link Image
Enzyme 3 GenAtlas ID BLVRA Link Image
Enzyme 3 HGNC ID HGNC:1062 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7p14-cen
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Maines MD, Polevoda BV, Huang TJ, McCoubrey WK Jr: Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes. Eur J Biochem. 1996 Jan 15;235(1-2):372-81. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Maines MD, Trakshel GM: Purification and characterization of human biliverdin reductase. Arch Biochem Biophys. 1993 Jan;300(1):320-6. [PubMed Link Image]
  4. Yamaguchi T, Komoda Y, Nakajima H: Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. J Biol Chem. 1994 Sep 30;269(39):24343-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5974
Enzyme 4 Name Flavin reductase
Enzyme 4 Synonyms
  1. FR
  2. NADPH-dependent diaphorase
  3. NADPH-flavin reductase
  4. FLR
  5. Biliverdin reductase B
  6. BVR-B
  7. Biliverdin-IX beta-reductase
  8. Green heme-binding protein
  9. GHBP
Enzyme 4 Gene Name BLVRB
Enzyme 4 Protein Sequence >Flavin reductase 
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAAD
VDKTVAGQDAVIVLLGTRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTK
VPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHD
LGHFMLRCLTTDEYDGHSTYPSHQYQ
Enzyme 4 Number of Residues 206
Enzyme 4 Molecular Weight 22120
Enzyme 4 Theoretical pI 7.76
Enzyme 4 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
—
Enzyme 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function Catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. Possible role in protecting cells from oxidative damage or in regulating iron metabolism. In the liver, converts biliverdin to bilirubin
Enzyme 4 Pathways
Enzyme 4 Reactions
  • reduced riboflavin + NADP+ = riboflavin + NADPH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1384068 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P30043 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name BLVRB_HUMAN Link Image
Enzyme 4 PDB ID 1HE5 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >621 bp 
ATGGCCGTCAAGAAGATCGCGATCTTCGGCGCCACTGGCCAGACCGGGCTCACCACCCTG
GCGCAGGCGGTGCAAGCAGGTTACGAAGTGACAGTGCTGGTGCGGGACTCCTCCAGGCTG
CCATCAGAGGGGCCCCGGCCGGCCCACGTGGTAGTGGGAGATGTTCTGCAGGCAGCCGAT
GTGGACAAGACCGTGGCTGGGCAGGACGCTGTCATCGTGCTGCTGGGCACCCGCAATGAC
CTCAGTCCCACGACAGTGATGTCCGAGGGCGCCCGGAACATTGTGGCAGCCATGAAGGCT
CATGGTGTGGACAAGGTCGTGGCCTGCACCTCGGCTTTCCTGCTCTGGGACCCTACCAAG
GTGCCCCCACGACTGCAGGCTGTGACTGATGACCACATCCGGATGCACAAGGTGCTGCGG
GAATCAGGCCTGAAGTACGTGGCTGTGATGCCGCCACACATAGGAGACCAGCCACTAACT
GGGGCGTACACAGTGACCCTGGATGGACGAGGGCCCTCAAGGGTCATCTCCAAACATGAC
CTGGGCCATTTCATGCTGCGCTGCCTCACCACCGATGAGTACGACGGACACAGCACCTAC
CCCTCCCACCAGTACCAGTAG
Enzyme 4 GenBank Gene ID D26308 Link Image
Enzyme 4 GeneCard ID BLVRB Link Image
Enzyme 4 GenAtlas ID BLVRB Link Image
Enzyme 4 HGNC ID HGNC:1063 Link Image
Enzyme 4 Chromosome Location 19
Enzyme 4 Locus 19q13.1-q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chikuba K, Yubisui T, Shirabe K, Takeshita M: Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1170-6. [PubMed Link Image]
  2. Komuro A, Tobe T, Hashimoto K, Nakano Y, Yamaguchi T, Nakajima H, Tomita M: Molecular cloning and expression of human liver biliverdin-IX beta reductase. Biol Pharm Bull. 1996 Jun;19(6):796-804. [PubMed Link Image]
  3. Yamaguchi T, Komuro A, Nakano Y, Tomita M, Nakajima H: Complete amino acid sequence of biliverdin-IX beta reductase from human liver. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1518-23. [PubMed Link Image]
  4. Yamaguchi T, Komoda Y, Nakajima H: Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. J Biol Chem. 1994 Sep 30;269(39):24343-8. [PubMed Link Image]
  5. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  6. Golaz O, Hughes GJ, Frutiger S, Paquet N, Bairoch A, Pasquali C, Sanchez JC, Tissot JD, Appel RD, Walzer C, et al.: Plasma and red blood cell protein maps: update 1993. Electrophoresis. 1993 Nov;14(11):1223-31. [PubMed Link Image]
  7. Shalloe F, Elliott G, Ennis O, Mantle TJ: Evidence that biliverdin-IX beta reductase and flavin reductase are identical. Biochem J. 1996 Jun 1;316 ( Pt 2):385-7. [PubMed Link Image]
  8. Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M: Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme. Nat Struct Biol. 2001 Mar;8(3):215-20. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13083
Enzyme 5 Name cDNA FLJ75742, highly similar to Homo sapiens biliverdin reductase A
Enzyme 5 Synonyms
  1. BLVRA, mRNA
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >cDNA FLJ75742, highly similar to Homo sapiens biliverdin reductase A 
MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLE
DALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKV
LHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLF
GELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLEN
VPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
Enzyme 5 Number of Residues 296
Enzyme 5 Molecular Weight 33429
Enzyme 5 Theoretical pI 6.41
Enzyme 5 GO Classification Not Available
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 Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158257156 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K747 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K747_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK291862 Link Image
Enzyme 5 GeneCard ID A8K747 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
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 15245
Enzyme 6 Name Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name ZNF554
Enzyme 6 Protein Sequence >Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c) 
MDFSQEEWELLEPAQKNLYREVMLENYRNVVSLEALKNQCTDVGIKEGPLSPAQTSQVTS
LSSWTGYLLFQPVASSHLEQREALWIEEKGTPQASCSDWMTVLRNQDSTYKKVALQEEPA
SGINMIKLIREDGGWKQLEDSHEDPQGLLSQKASLHVVAVPQEKATAWHGFGENGNLSPA
LVLSQGSSKGNHLCGSELDITSLASDSVLNHHQLGYADRRPCESNECGNAIRQNSHFIQH
GGKMFVYLENGQSLNHGMALTIHNKINTAEKPFECHQCGKVFNRRHSLSEHQRIHTGEKP
YECQECGRAFTHSSTLTRHLRTHTGEKPYGCGECGKAFNRISSLTQHQRIHTGEKPYKCE
DCGKSFCQSSYLILHKRTHTGEKPYECSECGKAFSDRSSLNQHERTHTGENPYECKQCGR
AFSQRSSLVRHERTHTGEKPYRCQECGKAFSQSSSLVTHQKTHSSQKTYKIIDCGKAFYQ
NRHLIGY
Enzyme 6 Number of Residues 487
Enzyme 6 Molecular Weight 54974
Enzyme 6 Theoretical pI 7.67
Enzyme 6 GO Classification Not Available
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 Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID A8MT35 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8MT35_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AC006130 Link Image
Enzyme 6 GeneCard ID A8MT35 Link Image
Enzyme 6 GenAtlas ID HMOX2 Link Image
Enzyme 6 HGNC ID HGNC:5014 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available