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Human Metabolome Database Version 2.5

 

Showing metabocard for 4-Methylpentanal (HMDB01318)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:40
Accession Number HMDB01318
Secondary Accession Numbers Not Available
Common Name 4-Methylpentanal
Description 4-Methylpentanal is an intermediate in the metabolism of C21-Steroid hormone. It is a substrate for Cytochrome P450 11A1 (mitochondrial).
Synonyms
  1. 4-Methyl valeraldehyde
  2. 4-Methylvaleraldehyde
  3. 4-methyl-Valeraldehyde
  4. 4-methylpentanal
  5. isocaproaldehyde: 4-methyl-Pentanal
  6. isohexana
Chemical IUPAC Name 4-methylpentanal
Chemical Formula C6H12O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Ketones and aldehydes
Class
  • Aldehydes
Sub Class
  • Short chain aldehydes
Family
  • Mammalian Metabolite
Species
  • aldehyde
Biofunction
  • Component of C21-Steroid hormone metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 100.159
Monoisotopic Molecular Weight 100.088814
Isomeric SMILES CC(C)CCC=O
Canonical SMILES CC(C)CCC=O
KEGG Compound ID C02373 Link Image
BioCyc ID 4-METHYLPENTANAL Link Image
BiGG ID 39716 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01318 Link Image
Metagene Link HMDB01318 Link Image
METLIN ID 6155 Link Image
PubChem Compound 129 Link Image
PubChem Substance 7888996 Link Image
ChEBI ID Not Available
CAS Registry Number 1119-16-0
InChI Identifier InChI=1/C6H12O/c1-6(2)4-3-5-7/h5-6H,3-4H2,1-2H3
Synthesis Reference Matsuura K; Deyashiki Y; Bunai Y; Ohya I; Hara A Aldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands. Archives of biochemistry and biophysics (1996), 328(2), 265-71.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.93 mg/mL [MEYLAN,WM et al. (1996)]; 3.80 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.92 [Predicted by ALOGPS]; 2.2 [Predicted by PubChem via XLOGP]; 1.73 [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
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Predicted 13C NMR Spectrum Show Image
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Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • mitochondria
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
Steroidogenesis SMP00130 Link Image map00140 Link Image
General References Not Available
Metabolic Enzymes
  1. Cytochrome P450 11A1, mitochondrial precursor
  2. cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
Enzyme 1 [top]
Enzyme 1 ID 5998
Enzyme 1 Name Cytochrome P450 11A1, mitochondrial precursor
Enzyme 1 Synonyms
  1. CYPXIA1
  2. P450(scc
  3. Cholesterol side-chain cleavage enzyme
  4. Cholesterol desmolase
Enzyme 1 Gene Name CYP11A1
Enzyme 1 Protein Sequence >Cytochrome P450 11A1, mitochondrial precursor 
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 1 Number of Residues 521
Enzyme 1 Molecular Weight 60103
Enzyme 1 Theoretical pI 9.18
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone
Enzyme 1 Pathways
Enzyme 1 Reactions
  • cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O
Enzyme 1 Pfam Domain Function Not Available
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181376 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P05108 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP11A_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1566 bp 
ATGCTGGCCAAGGGTCTTCCCCCACGCTCAGTCCTGGTCAAAGGCTACCAGACCTTTCTG
AGTGCCCCCAGGGAGGGGCTGGGGCGTCTCAGGGTGCCCACTGGCGAGGGAGCTGGCATC
TCCACCCGCAGTCCTCGCCCCTTCAATGAGATCCCCTCTCCTGGTGACAATGGCTGGCTA
AACCTGTACCATTTCTGGAGGGAGACGGGCACACACAAAGTCCACCTTCACCATGTCCAG
AATTTCCAGAAGTATGGCCCGATTTACAGGGAGAAGCTCGGCAACGTGGAGTCGGTTTAT
GTCATCGACCCTGAAGATGTGGCCCTTCTCTTTAAGTCCGAGGGCCCCAACCCAGAACGA
TTCCTCATCCCGCCCTGGGTCGCCTATCACCAGTATTACCAGAGACCCATAGGAGTCCTG
TTGAAGAAGTCGGCAGCCTGGAAGAAAGACCGGGTGGCCCTGAACCAGGAGGTGATGGCT
CCAGAGGCCACCAAGAACTTTTTGCCCCTGTTGGATGCAGTGTCTCGGGACTTCGTCAGT
GTCCTGCACAGGCGCATCAAGAAGGCGGGCTCCGGAAATTACTCGGGGGACATCAGTGAT
GACCTGTTCCGCTTTGCCTTTGAGTCCATCACTAACGTCATTTTTGGGGAGCGCCAGGGG
ATGCTGGAGGAAGTAGTGAACCCCGAGGCCCAGCGATTCATTGATGCCATCTACCAGATG
TTCCACACCAGCGTCCCCATGCTCAACCTTCCCCCAGACCTGTTCCGTCTGTTCAGGACC
AAGACCTGGAAGGACCATGTGGCTGCATGGGACGTGATTTTCAGTAAAGCTGACATATAC
ACCCAGAACTTCTACTGGGAATTGAGACAGAAAGGAAGTGTTCACCACGATTACCGTGGC
ATGCTCTACAGACTCCTGGGAGACAGCAAGATGTCCTTCGAGGACATCAAGGCCAACGTC
ACAGAGATGCTGGCAGGAGGGGTGGACACGACGTCCATGACCCTGCAGTGGCACTTGTAT
GAGATGGCACGCAACCTGAAGGTGCAGGATATGCTGCGGGCAGAGGTCTTGGCTGCGCGG
CACCAGGCCCAGGGAGACATGGCCACGATGCTACAGCTGGTCCCCCTCCTCAAAGCCAGC
ATCAAGGAGACACTAAGACTTCACCCCATCTCCGTGACCCTGCAGAGATATCTTGTAAAT
GACTTGGTTCTTCGAGATTACATGATTCCTGCCAAGACACTGGTGCAAGTGGCCATCTAT
GCTCTGGGCCGAGAGCCCACCTTCTTCTTCGACCCGGAAAATTTTGACCCAACCCGATGG
CTGAGCAAAGACAAGAACATCACCTACTTCCGGAACTTGGGCTTTGGCTGGGGTGTGCGG
CAGTGTCTGGGACGGCGGATCGCTGAGCTAGAGATGACCATCTTCCTCATCAATATGCTG
GAGAACTTCAGAGTTGAAATCCAACACCTCAGCGATGTGGGCACCACATTCAACCTCATT
CTGATGCCTGAAAAGCCCATCTCCTTCACCTTCTGGCCCTTTAACCAGGAAGCAACCCAG
CAGTGA
Enzyme 1 GenBank Gene ID M14565 Link Image
Enzyme 1 GeneCard ID CYP11A1 Link Image
Enzyme 1 GenAtlas ID CYP11A1 Link Image
Enzyme 1 HGNC ID HGNC:2590 Link Image
Enzyme 1 Chromosome Location 15
Enzyme 1 Locus 15q23-q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Chung BC, Matteson KJ, Voutilainen R, Mohandas TK, Miller WL: Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8962-6. [PubMed Link Image]
  2. Morohashi K, Sogawa K, Omura T, Fujii-Kuriyama Y: Gene structure of human cytochrome P-450(SCC), cholesterol desmolase. J Biochem (Tokyo). 1987 Apr;101(4):879-87. [PubMed Link Image]
  3. Hu MC, Guo IC, Lin JH, Chung BC: Regulated expression of cytochrome P-450scc (cholesterol-side-chain cleavage enzyme) in cultured cell lines detected by antibody against bacterially expressed human protein. Biochem J. 1991 Mar 15;274 ( Pt 3):813-7. [PubMed Link Image]
  4. Matteson KJ, Chung BC, Urdea MS, Miller WL: Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency causing congenital lipoid adrenal hyperplasia using bovine-sequence P450scc oligodeoxyribonucleotide probes. Endocrinology. 1986 Apr;118(4):1296-305. [PubMed Link Image]
  5. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  6. Tajima T, Fujieda K, Kouda N, Nakae J, Miller WL: Heterozygous mutation in the cholesterol side chain cleavage enzyme (p450scc) gene in a patient with 46,XY sex reversal and adrenal insufficiency. J Clin Endocrinol Metab. 2001 Aug;86(8):3820-5. [PubMed Link Image]
  7. Katsumata N, Ohtake M, Hojo T, Ogawa E, Hara T, Sato N, Tanaka T: Compound heterozygous mutations in the cholesterol side-chain cleavage enzyme gene (CYP11A) cause congenital adrenal insufficiency in humans. J Clin Endocrinol Metab. 2002 Aug;87(8):3808-13. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13012
Enzyme 2 Name cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
Enzyme 2 Synonyms
  1. CYP11A1, mRNA
  2. Cytochrome P450, family 11, subfamily A, polypeptide 1, isoform CRA_b
Enzyme 2 Gene Name CYP11A1
Enzyme 2 Protein Sequence >cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1 
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 2 Number of Residues 521
Enzyme 2 Molecular Weight 60103
Enzyme 2 Theoretical pI 9.18
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158258032 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8K8D5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8K8D5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AK292300 Link Image
Enzyme 2 GeneCard ID A8K8D5 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available