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How the glycosyltransferase OGT catalyzes amide bond cleavage.

ABSTRACT: The essential human enzyme O-linked ?-N-acetylglucosamine transferase (OGT), known for modulating the functions of nuclear and cytoplasmic proteins through serine and threonine glycosylation, was unexpectedly implicated in the proteolytic maturation of the cell cycle regulator host cell factor-1 (HCF-1). Here we show that HCF-1 cleavage occurs via glycosylation of a glutamate side chain followed by on-enzyme formation of an internal pyroglutamate, which undergoes spontaneous backbone hydrolysis.

SUBMITTER: Janetzko J

PROVIDER: S-EPMC5172607 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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How the glycosyltransferase OGT catalyzes amide bond cleavage.

Janetzko John J Trauger Sunia A SA Lazarus Michael B MB Walker Suzanne S

Nature chemical biology 20160912 11

The essential human enzyme O-linked β-N-acetylglucosamine transferase (OGT), known for modulating the functions of nuclear and cytoplasmic proteins through serine and threonine glycosylation, was unexpectedly implicated in the proteolytic maturation of the cell cycle regulator host cell factor-1 (HCF-1). Here we show that HCF-1 cleavage occurs via glycosylation of a glutamate side chain followed by on-enzyme formation of an internal pyroglutamate, which undergoes spontaneous backbone hydrolysis. ...[more]

PMID: 27618188

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