1apy: Difference between revisions
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Revision as of 15:45, 30 October 2007
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HUMAN ASPARTYLGLUCOSAMINIDASE
OverviewOverview
The high resolution crystal structure of human lysosomal, aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme, is synthesized as a single polypeptide precursor, which is immediately, post-translationally cleaved into alpha- and beta-subunits. Two alpha- and, beta-chains are found to pack together forming the final heterotetrameric, structure. The catalytically essential residue, the N-terminal threonine, of the beta-chain is situated in the deep pocket of the funnel-shaped, active site. On the basis of the structure of the enzyme-product complex, we present a catalytic mechanism for this lysosomal enzyme with an, exceptionally high pH optimum. The three-dimensional structure also allows, the prediction of the structural consequences of human mutations resulting, in ... [(full description)]
About this StructureAbout this Structure
1APY is a [Single protein] structure of sequence from [Homo sapiens] with NAG as [ligand]. Active as [N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [3.5.1.26]. Structure known Active Sites: B1 and D1. Full crystallographic information is available from [OCA].
ReferenceReference
Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222
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