Biology:Trans-L-3-hydroxyproline dehydratase: Difference between revisions
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Latest revision as of 08:33, 11 February 2024
| trans-L-3-hydroxyproline dehydratase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.2.1.77 | ||||||||
| 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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The enzyme trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) catalyzes the chemical reaction
- trans-L-3-hydroxyproline Δ1-pyrroline 2-carboxylate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is trans-L-3-hydroxyproline hydro-lyase (Δ1-pyrroline-2-carboxylate-forming). This enzyme is also called trans-L-3-hydroxyproline hydro-lyase.
References
- "Conversion of 3-hydroxyproline to proline in the rat requires reduced pyridine-nucleotides". Fed. Proc. 42: 2232. 1983.
- "Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes". The Journal of Biological Chemistry 287 (26): 21654–62. June 2012. doi:10.1074/jbc.m112.363218. PMID 22528483.
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