Methylornithine synthase
| Methylornithine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.58 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Methylornithine synthase (EC 5.4.99.58, PylB) is an enzyme with systematic name L-lysine carboxy-aminomethylmutase.[1][2] This enzyme catalyses the conversion of L-lysine into (3R)-3-methyl-D-ornithine.
The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical enzymes.
References[]
- ^ Gaston MA, Zhang L, Green-Church KB, Krzycki JA (March 2011). "The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine". Nature. 471 (7340): 647–50. Bibcode:2011Natur.471..647G. doi:10.1038/nature09918. PMC 3070376. PMID 21455182.
- ^ Quitterer F, List A, Eisenreich W, Bacher A, Groll M (February 2012). "Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis". Angewandte Chemie. 51 (6): 1339–42. doi:10.1002/anie.201106765. PMID 22095926.
External links[]
- Methylornithine+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
Categories:
- EC 5.4.99