1apy: Difference between revisions

Revision as of 17:22, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1apy.png

Template:STRUCTURE 1apy

HUMAN ASPARTYLGLUCOSAMINIDASEHUMAN ASPARTYLGLUCOSAMINIDASE

Template:ABSTRACT PUBMED 8846222

About this StructureAbout this Structure

1APY is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Mon Jun 30 17:22:43 2008

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OCA

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-'''HUMAN ASPARTYLGLUCOSAMINIDASE'''
+===HUMAN ASPARTYLGLUCOSAMINIDASE===
-==Overview==
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-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 aspartylglucosaminuria (AGU), a lysosomal storage disease.
+The line below this paragraph, {{ABSTRACT_PUBMED_8846222}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8846222}}
 ==About this Structure==
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 [[Category: Glycosylasparaginase]]
 [[Category: Hydrolase]]
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