2gac
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T152C MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM
OverviewOverview
Glycosylasparaginase (GA) is a member of a novel family of N-terminal, nucleophile hydrolases that catalytically use an N-terminal residue as, both a polarizing base and a nucleophile. These enzymes are activated from, a single chain precursor by intramolecular autoproteolysis to yield the, N-terminal nucleophile. A deficiency of GA results in the human genetic, disorder known as aspartylglycosaminuria. In this study, we report the, crystal structure of recombinant GA from Flavobacterium meningosepticum., Similar to the human structure, the bacterial GA forms an, alphabetabetaalpha sandwich. However, some significant differences are, observed between the Flavobacterium and human structures. The active site, of Flavobacterium glycosylasparaginase is in an open conformation when, compared ... [(full description)]
About this StructureAbout this Structure
2GAC is a [Protein complex] structure of sequences from [Elizabethkingia meningoseptica]. Active as [N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [3.5.1.26]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis., Guo HC, Xu Q, Buckley D, Guan C, J Biol Chem. 1998 Aug 7;273(32):20205-12. PMID:9685368
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