1apy

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[[Image:1apy.gif|left|200px]]
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{{STRUCTURE_1apy| PDB=1apy | SCENE= }}
{{STRUCTURE_1apy| PDB=1apy | SCENE= }}
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'''HUMAN ASPARTYLGLUCOSAMINIDASE'''
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===HUMAN ASPARTYLGLUCOSAMINIDASE===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8846222 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8846222}}
==About this Structure==
==About this Structure==
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[[Category: Glycosylasparaginase]]
[[Category: Glycosylasparaginase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:34:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:22:43 2008''

Revision as of 14:22, 30 June 2008

Image:1apy.png

Template:STRUCTURE 1apy

HUMAN ASPARTYLGLUCOSAMINIDASE

Template:ABSTRACT PUBMED 8846222

About this Structure

1APY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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