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Methylthioribulose 1-phosphate dehydratase

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methylthioribulose 1-phosphate dehydratase
X-ray structure of human methylthioribulose 1-phosphate dehydratase (APIP). PDB entry 4m6r[1]
Identifiers
EC no.4.2.1.109
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BRENDABRENDA entry
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MetaCycmetabolic pathway
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The enzyme methylthioribulose 1-phosphate dehydratase (EC .2.1.109) catalyzes the chemical reaction

5-(methylsulfanyl)-D)ribulose 1-phosphate 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 [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]. 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

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  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.