1zs9

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{{STRUCTURE_1zs9| PDB=1zs9 | SCENE= }}
{{STRUCTURE_1zs9| PDB=1zs9 | SCENE= }}
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'''Crystal structure of human enolase-phosphatase E1'''
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===Crystal structure of human enolase-phosphatase E1===
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==Overview==
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Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively. The structures support the proposed mechanism of phosphatase activity and further suggest the probable mechanism of enolization. We establish a model for substrate binding to describe in detail the enzymatic reaction and the formation of the transition state, which will provide insight into the reaction mechanisms of other enzymes in the same family.
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(as it appears on PubMed at http://www.pubmed.gov), where 15843022 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15843022}}
==About this Structure==
==About this Structure==
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[[Category: Wang, H.]]
[[Category: Wang, H.]]
[[Category: Structure human enolase-phosphatase e1]]
[[Category: Structure human enolase-phosphatase e1]]
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Revision as of 13:00, 28 July 2008

Image:1zs9.png

Template:STRUCTURE 1zs9

Crystal structure of human enolase-phosphatase E1

Template:ABSTRACT PUBMED 15843022

About this Structure

1ZS9 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1wdh. Full crystallographic information is available from OCA.

Reference

Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity., Wang H, Pang H, Bartlam M, Rao Z, J Mol Biol. 2005 May 13;348(4):917-26. PMID:15843022

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