Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks.

doi:10.1074/jbc.M204413200

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Article

Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks.

The Journal of biological chemistry - 26 Jul 2002

Thoden James B, Henderson Jenny M, Fridovich-Keil Judith L, Holden Hazel M

Abstract excerpt

UDP-galactose 4-epimerase catalyzes the interconversion of UDP-Gal and UDP-Glc during normal galactose metabolism. The mammalian form of the enzyme, unlike its Escherichia coli counterpart, can also interconvert UDP-GalNAc and UDP-GlcNAc. One key feature of the epimerase reaction mechanism is the rotation of a 4-ketopyranose intermediate in the active site. By comparing the high resolution x-ray structures of...

Topics

Crystallography, X-Ray
Escherichia coli
Humans
Models, Chemical
Models, Molecular
Mutation
Plasmids
Protein Conformation
Tyrosine
UDPglucose 4-Epimerase
X-Rays

Source

Open in PubMed

Identifiers

PMID: 12019271
DOI: 10.1074/jbc.M204413200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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