Misplaced Pages

Methylthioribulose 1-phosphate dehydratase

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
methylthioribulose 1-phosphate dehydratase
X-ray structure of human methylthioribulose 1-phosphate dehydratase (APIP). PDB entry 4m6r
Identifiers
EC no.4.2.1.109
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme methylthioribulose 1-phosphate dehydratase (EC .2.1.109) catalyzes the chemical reaction

5-(methylsulfanyl)-D)ribulose 1-phosphate {\displaystyle \rightleftharpoons } 5-(methylthio)-2,3-dioxopentyl phosphate + H2

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 5-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase . Other names in common use include 1-PMT-ribulose dehydratase, and S-methyl-5-thio-D-ribulose-1-phosphate hydro-lyase. This enzyme participates in methionine metabolism.

References

  1. Kang, W; Hong, S. H.; Lee, H. M.; Kim, N. Y.; Lim, Y. C.; Le Le, T. M.; Lim, B; Kim, H. C.; Kim, T. Y.; Ashida, H; Yokota, A; Hah, S. S.; Chun, K. H.; Jung, Y. K.; Yang, J. K. (2014). "Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme". Proceedings of the National Academy of Sciences. 111 (1): E54-61. Bibcode:2014PNAS..111E..54K. doi:10.1073/pnas.1308768111. PMC 3890807. PMID 24367089.
Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases
4.2.2: Acting on polysaccharides
4.2.3: Acting on phosphates
4.2.99: Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:


This EC 4.2 enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

Categories: