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Crystal Structures of Orotidine Monophosphate Decarboxylase: Does the Structure Reveal the Mechanism of Nature's Most Proficient Enzyme?
Author(s) -
Houk Kendall N.,
Lee Jeehiun K.,
Tantillo Dean J.,
Bahmanyar Sogole,
Hietbrink Bruce N.
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010202)2:2<113::aid-cbic113>3.0.co;2-t
Subject(s) - mechanism (biology) , enzyme , chemistry , crystal structure , biochemistry , stereochemistry , crystallography , physics , quantum mechanics
The mystery of proficiency remains: The recently solved crystal structures of free orotidine monophosphate decarboxylase (ODCase) and of the enzyme in complex with inhibitors reveal unusual structural features. However, despite the similarities among the structures, several startling new mechanisms of action have been proposed to explain how ODCase achieves its spectacular catalytic proficiency in catalyzing the decarboxylation of OMP ( 1 ) to UMP ( 2 ). R = ribose 5′‐monophosphate.