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Human Metabolome Database Version 2.5

 

Showing metabocard for 3a,7a,12a,24-Tetrahydroxy-5b-cholestanoyl-CoA (HMDB06890)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-14 19:05:41
Update Date 2010-04-26 16:22:25
Accession Number HMDB06890
Secondary Accession Numbers Not Available
Common Name 3a,7a,12a,24-Tetrahydroxy-5b-cholestanoyl-CoA
Description 3a,7a,12a,24-Tetrahydroxy-5b-cholestanoyl-CoA is an intermediate in bile acid synthesis. Bile acids are steroid acids found predominantly in bile of mammals. The distinction between different bile acids is minute, depends only on presence or absence of hydroxyl groups on positions 3, 7, and 12. Bile acids are physiological detergents that facilitate excretion, absorption, and transport of fats and sterols in the intestine and liver. Bile acids are also steroidal amphipathic molecules derived from the catabolism of cholesterol. They modulate bile flow and lipid secretion, are essential for the absorption of dietary fats and vitamins, and have been implicated in the regulation of all the key enzymes involved in cholesterol homeostasis. Bile acids recirculate through the liver, bile ducts, small intestine and portal vein to form an enterohepatic circuit. They exist as anions at physiological pH and, consequently, require a carrier for transport across the membranes of the enterohepatic tissues. The unique detergent properties of bile acids are essential for the digestion and intestinal absorption of hydrophobic nutrients. Bile acids have potent toxic properties (e.g., membrane disruption) and there are a plethora of mechanisms to limit their accumulation in blood and tissues. (PMID: 11316487, 16037564, 12576301, 11907135)
Synonyms
  1. 3alpha,7alpha,12alpha,24zeta-Tetrahydroxy-5beta-cholestanoyl-CoA
  2. 3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-Coenzyme A
  3. 3a,7a,12a,24-Tetrahydroxy-5b-cholestanoyl-CoA
  4. 3a,7a,12a,24-Tetrahydroxy-5b-cholestanoyl-Coenzyme A
  5. 3alpha,7alpha,12alpha,24zeta-Tetrahydroxy-5beta-cholestanoyl-Coenzyme A
  6. 3a,7a,12a,24z-Tetrahydroxy-5b-cholestanoyl-CoA
  7. 3a,7a,12a,24z-Tetrahydroxy-5b-cholestanoyl-Coenzyme A
  8. 3alpha,7alpha,12alpha,24-Tetrahydroxy-5beta-cholestanoyl-CoA
  9. (24R,25R)-3-alpha,7-alpha,12-alpha,24- tetrahydroxy-5-beta-cholestanoyl-CoA
  10. (24R,25R)-3-alpha,7-alpha,12-alpha,24- tetrahydroxy-5-beta-cholestanoyl-Coenzyme A
Chemical IUPAC Name 3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-{[3-oxo-3-({2-[(3a,7a,12a,24-tetrahydroxy-5b-cholestan-26-oyl)sulfanyl]ethyl}amino)propyl]amino}butyl] dihydrogen diphosphate}
Chemical Formula C48H80N7O21P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Long chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 1216.169
Monoisotopic Molecular Weight 1215.434082
Isomeric SMILES CC(CCC(O)C(C)C(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C1CCC2C3[C@H](O)C[C@@H]4C[C@H](O)CCC4(C)C3C[C@H](O)C12C
Canonical SMILES CC(CCC(O)C(C)C(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C1CCC2C3C(O)CC4CC(O)CCC4(C)C3CC(O)C12C
KEGG Compound ID C05450 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06890 Link Image
Metagene Link HMDB06890 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance 7812 Link Image
ChEBI ID 27458 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C48H80N7O21P3S/c1-24(28-8-9-29-36-30(19-34(59)48(28,29)6)47(5)13-11-27(56)17-26(47)18-32(36)58)7-10-31(57)25(2)45(64)80-16-15-50-35(60)12-14-51-43(63)40(62)46(3,4)21-73-79(70,71)76-78(68,69)72-20-33-39(75-77(65,66)67)38(61)44(74-33)55-23-54-37-41(49)52-22-53-42(37)55/h22-34,36,38-40,44,56-59,61-62H,7-21H2,1-6H3,(H,50,60)(H,51,63)(H,68,69)(H,70,71)(H2,49,52,53)(H2,65,66,67)/t24?,25?,26-,27+,28?,29?,30?,31?,32+,33+,34-,36?,38+,39+,40?,44+,47?,48?/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.18 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.65 [Predicted by ALOGPS] 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 Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
General References Not Available
Metabolic Enzymes
  1. Peroxisomal multifunctional enzyme type 2
  2. Retinol dehydrogenase 13
  3. Isobutyryl-CoA dehydrogenase, mitochondrial precursor
Enzyme 1 [top]
Enzyme 1 ID 5716
Enzyme 1 Name Peroxisomal multifunctional enzyme type 2
Enzyme 1 Synonyms
  1. MFE-2
  2. D-bifunctional protein
  3. DBP
  4. 17-beta-hydroxysteroid dehydrogenase 4
  5. 17-beta-HSD 4
  6. D-3-hydroxyacyl-CoA dehydratase
  7. 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
  8. 3- hydroxyacyl-CoA dehydrogenase
Enzyme 1 Gene Name HSD17B4
Enzyme 1 Protein Sequence >Peroxisomal multifunctional enzyme type 2 
MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVE
EIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIH
RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAI
EGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVG
AGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLS
KIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKD
LKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRA
GKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKV
AVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFS
ARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISN
AYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNI
GAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNI
MLSQKLQMILKDYAKL
Enzyme 1 Number of Residues 736
Enzyme 1 Molecular Weight 79687
Enzyme 1 Theoretical pI 9.21
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid binding
  • sterol carrier activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1050517 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P51659 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DHB4_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2211 bp 
ATGGGCTCACCGCTGAGGTTCGACGGGCGGGTGGTACTGGTCACCGGCGCGGGGGCAGGA
TTGGGCCGAGCCTATGCCCTGGCTTTTGCAGAAAGAGGAGCGTTAGTTGTTGTGAATGAT
TTGGGAGGGGACTTCAAAGGAGTTGGTAAAGGCTCCTTAGCTGCTGATAAGGTTGTTGAA
GAAATAAGAAGGAGAGGTGGAAAAGCAGTGGCCAACTATGATTCAGTGGAAGAAGGAGAG
AAGGTTGTGAAGACAGCCCTGGATGCTTTTGGAAGAATAGATGTTGTGGTCAACAATGCT
GGAATTCTGAGGGATCGTTCCTTTGCTAGGATAAGTGATGAAGACTGGGATATAATCCAC
AGAGTTCATTTGCGGGGTTCATTCCAAGTGACACGGGCAGCATGGGAACACATGAAGAAA
CAGAAGTATGGAAGGATTATTATGACTTCATCAGCTTCAGGAATATATGGCAACTTTGGC
CAGGCCAATTATAGTGCTGCAAAGTTGGGTCTTCTGGGCCTTGCAAATTCTCTTGCAATT
GAAGGCAGGAAAAGCAACATTCATTGTAACACCATTGCTCCTAATGCGGGATCACGGATG
ACTCAGACAGTTATGCCTGAAGATCTTGTGGAAGCCCTGAAGCCAGAGTATGTGGCACCT
CTTGTCCTTTGGCTTTGTCACGAGAGTTGTGAGGAGAATGGTGGCTTGTTTGAGGTTGGA
GCAGGATGGATTGGAAAATTACGCTGGGAGCGGACTCTTGGAGCTATTGTAAGACAAAAG
AATCACCCAATGACTCCTGAGGCAGTCAAGGCTAACTGGAAGAAGATCTGTGACTTTGAG
AATGCCAGCAAGCCTCAGAGTATCCAAGAATCAACTGGCAGTATAATTGAAGTTCTGAGT
AAAATAGATTCAGAAGGAGGAGTTTCAGCAAATCATACTAGTCGTGCAACGTCTACAGCA
ACATCAGGATTTGCTGGAGCTATTGGCCAGAAACTCCCTCCATTTTCTTATGCTTATACG
GAACTGGAAGCTATTATGTATGCCCTTGGAGTGGGAGCGTCAATCAAGGATCCAAAAGAT
TTGAAATTTATTTATGAAGGAAGTTCTGATTTCTCCTGTTTGCCCACCTTCGGAGTTATC
ATAGGTCAGAAATCTATGATGGGTGGAGGATTAGCAGAAATTCCTGGACTTTCAATCAAC
TTTGCAAAGGTTCTTCATGGAGAGCAGTACTTAGAGTTATATAAACCACTTCCCAGAGCA
GGAAAATTAAAATGTGAAGCAGTTGTTGCTGATGTCCTAGATAAAGGATCCGGTGTAGTG
ATTATTATGGATGTCTATTCTTATTCTGAGAAGGAACTTATATGCCACAATCAGTTCTCT
CTCTTTCTTGTTGGCTCTGGAGGCTTTGGTGGAAAACGGACATCAGACAAAGTCAAGGTA
GCTGTAGCCATACCTAATAGACCTCCTGATGCTGTACTTACAGATACCACCTCTCTTAAT
CAGGCTGCTTTGTACCGCCTCAGTGGAGACTGGAATCCCTTACACATTGATCCTAACTTT
GCTAGTCTAGCAGGTTTTGACAAGCCCATATTACATGGATTATGTACATTTGGATTTTCT
GCCAGGCGTGTGTTACAGCAGTTTGCAGATAATGATGTGTCAAGATTCAAGGCAATTAAG
GCTCGTTTTGCAAAACCAGTATATCCAGGACAAACTCTACAAACTGAGATGTGGAAGGAA
GGAAACAGAATTCATTTTCAAACCAAGGTCCAAGAAACTGGAGACATTGTCATTTCAAAT
GCATATGTGGATCTTGCACCAACATCTGGTACTTCAGCTAAGACACCCTCTGAGGGCGGG
AAGCTTCAGAGTACCTTTGTATTTGAGGAAATAGGACGCCGCCTAAAGGATATTGGGCCT
GAGGTGGTGAAGAAAGTAAATGCTGTATTTGAGTGGCATATAACCAAAGGCGGAAATATT
GGGGCTAAGTGGACTATTGACCTGAAAAGTGGTTCTGGAAAAGTGTACCAAGGCCCTGCA
AAAGGTGCTGCTGATACAACAATCATACTTTCAGATGAAGATTTCATGGAGGTGGTCCTG
GGCAAGCTTGACCCTCAGAAGGCATTCTTTAGTGGCAGGCTGAAGGCCAGAGGGAACATC
ATGCTGAGCCAGAAACTTCAGATGATTCTTAAAGACTACGCCAAGCTCTGA
Enzyme 1 GenBank Gene ID X87176 Link Image
Enzyme 1 GeneCard ID HSD17B4 Link Image
Enzyme 1 GenAtlas ID HSD17B4 Link Image
Enzyme 1 HGNC ID HGNC:5213 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Adamski J, Normand T, Leenders F, Monte D, Begue A, Stehelin D, Jungblut PW, de Launoit Y: Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. Biochem J. 1995 Oct 15;311 ( Pt 2):437-43. [PubMed Link Image]
  2. Jiang LL, Miyazawa S, Souri M, Hashimoto T: Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J Biochem (Tokyo). 1997 Feb;121(2):364-9. [PubMed Link Image]
  3. Leenders F, Dolez V, Begue A, Moller G, Gloeckner JC, de Launoit Y, Adamski J: Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV. Mamm Genome. 1998 Dec;9(12):1036-41. [PubMed Link Image]
  4. Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T: Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J Biochem (Tokyo). 1996 Sep;120(3):624-32. [PubMed Link Image]
  5. Haapalainen AM, van Aalten DM, Merilainen G, Jalonen JE, Pirila P, Wierenga RK, Hiltunen JK, Glumoff T: Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. J Mol Biol. 2001 Nov 9;313(5):1127-38. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8823
Enzyme 2 Name Retinol dehydrogenase 13
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name RDH13
Enzyme 2 Protein Sequence >Retinol dehydrogenase 13 
MSRYLLPLSALGTVAGAAVLLKDYVTGGACPSKATIPGKTVIVTGANTGIGKQTALELAR
RGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDI
LINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAG
HIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH
TGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEA
EDEEVARRLWAESARLVGLEAPSVREQPLPR
Enzyme 2 Number of Residues 331
Enzyme 2 Molecular Weight 35933
Enzyme 2 Theoretical pI 8.24
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Does not exhibit retinol dehydrogenase (RDH) activity in vitro
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-17
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 22761451 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8NBN7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name RDH13_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >996 bp 
ATGAGCCGCTACCTGCTGCCGCTGTCGGCGCTGGGCACGGTAGCAGGCGCCGCCGTGCTG
CTCAAGGACTATGTCACCGGTGGGGCTTGCCCCAGCAAGGCCACCATCCCTGGGAAGACG
GTCATCGTGACGGGCGCCAACACAGGCATCGGGAAGCAGACCGCCTTGGAACTGGCCAGG
AGAGGAGGCAACATCATCCTGGCCTGCCGAGACATGGAGAAGTGTGAGGCGGCAGCAAAG
GACATCCGCGGGGAGACCCTCAATCACCATGTCAACGCCCGGCACCTGGACTTGGCTTCC
CTCAAGTCTATCCGAGTGTTTGCAGCAAAGATCATTGAAGAGGAGGAGCGAGTGGACATT
CTAATCAACAACGCGGGTGTGATGCGGTGCCCCCACTGGACCACCGAGGACGGCTTCGAG
ATGCAGTTTGGCGTTAACCACCTGGGTCACTTTCTCTTGACAAACTTGCTGCTGGACAAG
CTGAAAGCCTCAGCCCCTTCGCGGATCATCAACCTCTCGTCCCTGGCCCATGTTGCTGGG
CACATAGACTTTGACGACTTGAACTGGCAGACGAGGAAGTATAACACCAAAGCCGCCTAC
TGCCAGAGCAAGCTCGCCATCGTCCTCTTCACCAAGGAGCTGAGCCGGCGGCTGCAAGGC
TCTGGTGTGACTGTCAACGCCCTGCACCCCGGCGTGGCCAGGACAGAGCTGGGCAGACAC
ACGGGCATCCATGGCTCCACCTTCTCCAGCACCACACTCGGGCCCATCTTCTGGCTGCTG
GTCAAGAGCCCCGAGCTGGCCGCCCAGCCCAGCACATACCTGGCCGTGGCGGAGGAACTG
GCGGATGTTTCCGGAAAGTACTTCGATGGACTCAAACAGAAGGCCCCGGCCCCCGAGGCT
GAGGATGAGGAGGTGGCCCGGAGGCTTTGGGCTGAAAGTGCCCGCCTGGTGGGCTTAGAG
GCTCCCTCTGTGAGGGAGCAGCCCCTCCCCAGATAA
Enzyme 2 GenBank Gene ID AK075392 Link Image
Enzyme 2 GeneCard ID RDH13 Link Image
Enzyme 2 GenAtlas ID RDH13 Link Image
Enzyme 2 HGNC ID HGNC:19978 Link Image
Enzyme 2 Chromosome Location 19
Enzyme 2 Locus 19q13.42
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Haeseleer F, Jang GF, Imanishi Y, Driessen CA, Matsumura M, Nelson PS, Palczewski K: Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina. J Biol Chem. 2002 Nov 22;277(47):45537-46. Epub 2002 Sep 10. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 10872
Enzyme 3 Name Isobutyryl-CoA dehydrogenase, mitochondrial precursor
Enzyme 3 Synonyms
  1. Acyl-CoA dehydrogenase family member 8
  2. ACAD-8
  3. Activator-recruited cofactor 42 kDa component
  4. ARC42
Enzyme 3 Gene Name ACAD8
Enzyme 3 Protein Sequence >Isobutyryl-CoA dehydrogenase, mitochondrial precursor 
MLWSGCRRFGARLGCLPGGLRVLVQTGHRSLTSCIDPSMGLNEEQKEFQKVAFDFAAREM
APNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT
AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQG
DHYILNGSKAFISGAGESDIYVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNS
QPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLN
VRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD
ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE
Enzyme 3 Number of Residues 415
Enzyme 3 Molecular Weight 45070
Enzyme 3 Theoretical pI Not Available
Enzyme 3 GO Classification
Function
  • acyl-CoA dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • Flavin adenine dinucleotide oxidized + Propanoyl-CoA --> Flavin adenine dinucleotide reduced + Propenoyl-CoA
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 6465955 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9UKU7 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACAD8_HUMAN Link Image
Enzyme 3 PDB ID 1RX0 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 AF126245 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID ACAD8 Link Image
Enzyme 3 HGNC ID HGNC:87 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Telford EA, Moynihan LM, Markham AF, Lench NJ: Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family. Biochim Biophys Acta. 1999 Sep 3;1446(3):371-6. [PubMed Link Image]
  2. Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed Link Image]
  3. Naar AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R: Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 1999 Apr 29;398(6730):828-32. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available