2vlb

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{{STRUCTURE_2vlb| PDB=2vlb | SCENE= }}
{{STRUCTURE_2vlb| PDB=2vlb | SCENE= }}
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'''STRUCTURE OF UNLIGANDED ARYLMALONATE DECARBOXYLASE'''
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===STRUCTURE OF UNLIGANDED ARYLMALONATE DECARBOXYLASE===
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==Overview==
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Arylmalonate decarboxylase (AMDase) from Bordetella bronchiseptica catalyzes the enantioselective decarboxylation of arylmethylmalonates without the need for an organic cofactor or metal ion. The decarboxylation reaction is of interest for the synthesis of fine chemicals. As basis for an analysis of the catalytic mechanism of AMDase and for a rational enzyme design, we determined the X-ray structure of the enzyme up to 1.9 A resolution. Like the distantly related aspartate or glutamate racemases, AMDase has an aspartate transcarbamoylase fold consisting of two alpha/beta domains related by a pseudo dyad. However, the domain orientation of AMDase differs by about 30 degrees from that of the glutamate racemases, and also significant differences in active-site structures are observed. In the crystals, four independent subunits showing different conformations of active-site loops are present. This finding is likely to reflect the active-site mobility necessary for catalytic activity.
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{{ABSTRACT_PUBMED_18258259}}
==About this Structure==
==About this Structure==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Protein dynamic]]
[[Category: Protein dynamic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:59:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:47:42 2008''

Revision as of 09:47, 27 July 2008

Template:STRUCTURE 2vlb

STRUCTURE OF UNLIGANDED ARYLMALONATE DECARBOXYLASE

Template:ABSTRACT PUBMED 18258259

About this Structure

2VLB is a Single protein structure of sequence from Bordetella bronchiseptica. Full crystallographic information is available from OCA.

Reference

Active-site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchiseptica., Kuettner EB, Keim A, Kircher M, Rosmus S, Strater N, J Mol Biol. 2008 Mar 21;377(2):386-94. Epub 2008 Jan 5. PMID:18258259

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