Misplaced Pages

S-methyl-5-thioribose-1-phosphate isomerase

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.
S-methyl-5-thioribose-1-phosphate isomerase
Identifiers
EC no.5.3.1.23
CAS no.91608-95-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a S-methyl-5-thioribose-1-phosphate isomerase (EC 5.3.1.23) is an enzyme that catalyzes the chemical reaction

S-methyl-5-thio-alpha-D-ribose 1-phosphate {\displaystyle \rightleftharpoons } S-methyl-5-thio-D-ribulose 1-phosphate

Hence, this enzyme has one substrate, S-methyl-5-thio-alpha-D-ribose 1-phosphate, and one product, S-methyl-5-thio-D-ribulose 1-phosphate.

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase. Other names in common use include methylthioribose 1-phosphate isomerase, 1-PMTR isomerase, 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate, aldose-ketose-isomerase, 1-phospho-5'-S-methylthioribose isomerase, and S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase. This enzyme participates in methionine metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1T9K and 1W2W.

References

Isomerases: intramolecular oxidoreductases (EC 5.3)
5.3.1: Aldoses/Ketoses
5.3.2: Keto/Enol
5.3.3: C = C
5.3.4: S-S
5.3.99: other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:


This isomerase article is a stub. You can help Misplaced Pages by expanding it.

Categories: