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Article

The structural basis for a coordinated reaction catalyzed by a bifunctional glycosyltransferase in chondroitin biosynthesis.

The Journal of biological chemistry - 19 Oct 2012

Sobhany Mack, Kakuta Yoshimitsu, Sugiura Nobuo, Kimata Koji, Negishi Masahiko

Abstract excerpt

Bifunctional chondroitin synthase K4CP catalyzes glucuronic acid and N-acetylgalactosamine transfer activities and polymerizes a chondroitin chain. Here we have determined that an N-terminal region (residues 58-134) coordinates two transfer reactions and enables K4CP to catalyze polymerization. When residues 58-107 are deleted, K4CP loses polymerase activity while retaining both transfer activities. Peptide...

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Amino Acid Motifs
Catalysis
Escherichia coli
Glycosylation
Hexosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Tertiary

Structure-Activity Relationship

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Identifiers

PMID: 22936799
DOI: 10.1074/jbc.M112.375873
PMCID: PMC3476270

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