17-alpha-hydroxyprogesterone aldolase
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17α-Hydroxyprogesterone aldolase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.2.30 | ||||||||
CAS no. | 62213-24-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 17α-hydroxyprogesterone aldolase (EC 4.1.2.30) is an enzyme that catalyzes the chemical reaction
- 17α-hydroxyprogesterone androst-4-en-3,17-dione + acetaldehyde
Hence, this enzyme has one substrate, 17α-hydroxyprogesterone, and two products, androst-4-en-3,17-dione and acetaldehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 17α-hydroxyprogesterone acetaldehyde-lyase (4-androstene-3,17-dione-forming). Other names in common use include C-17/C-20-lyase, and 17α-hydroxyprogesterone acetaldehyde-lyase. This enzyme participates in androgen and estrogen metabolism.
References
[edit]- Nowotny E, Sananez RD, Nattero G, Yantorno C, Faillaci MG (1974). "Bioconversion of steroids in vitro by testes from autoimmunized rabbits". Hoppe-Seyler's Z. Physiol. Chem. 355 (6): 716–20. doi:10.1515/bchm2.1974.355.1.716. PMID 4435747.