CATH Classification

Domain Context

CATH Clusters

Superfamily alpha/beta hydrolase
Functional Family 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase

Enzyme Information

3.7.1.8
2,6-dioxo-6-phenylhexa-3-enoate hydrolase.
based on mapping to UniProt P9WNH4
2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate.
-!- Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 by ring-fission at a -CO-C bond. -!- Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
3.7.1.17
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase.
based on mapping to UniProt P9WNH4
(1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4- oate + H(2)O = 3-((3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4- yl)propanoate + (2Z,4Z)-2-hydroxyhexa-2,4-dienoate.
-!- The enzyme is involved in the bacterial degradation of the steroid ring structure, and is involved in degradation of multiple steroids, such as testosterone, cholesterol, and sitosterol.

UniProtKB Entries (1)

P9WNH4
HSAD_MYCTO
Mycobacterium tuberculosis CDC1551
4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase

PDB Structure

PDB 5JZ9
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Investigation of the mycobacterial enzyme HsaD as a potential novel target for anti-tubercular agents using a fragment-based drug design approach.
Ryan, A., Polycarpou, E., Lack, N.A., Evangelopoulos, D., Sieg, C., Halman, A., Bhakta, S., Eleftheriadou, O., McHugh, T.D., Keany, S., Lowe, E.D., Ballet, R., Abuhammad, A., Jacobs, W.R., Ciulli, A., Sim, E.
Br. J. Pharmacol.