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1tzj

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[[Image:1tzj.gif|left|200px]]
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{{STRUCTURE_1tzj| PDB=1tzj | SCENE= }}
{{STRUCTURE_1tzj| PDB=1tzj | SCENE= }}
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'''Crystal Structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine'''
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===Crystal Structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine===
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==Overview==
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1-Aminocyclopropane-1-carboxylate (ACC) deaminase is a pyridoxal 5'-phosphate (PLP) dependent enzyme catalyzing the opening of the cyclopropane ring of ACC to give alpha-ketobutyric acid and ammonia as the products. This ring cleavage reaction is unusual because the substrate, ACC, contains no abstractable alpha-proton and the carboxyl group is retained in the product. How the reaction is initiated to generate an alpha-carbanionic intermediate, which is the common entry for most PLP-dependent reactions, is not obvious. To gain insight into this unusual ring-opening reaction, we have solved the crystal structures of ACC deaminase from Pseudomonas sp. ACP in complex with substrate ACC, an inhibitor, 1-aminocyclopropane-1-phosphonate (ACP), the product alpha-ketobutyrate, and two d-amino acids. Several notable observations of these structural studies include the following: (1) a typically elusive gem-diamine intermediate is trapped in the enzyme complex with ACC or ACP; (2) Tyr294 is in close proximity (3.0 A) to the pro-S methylene carbon of ACC in the gem-diamine complexes, implicating a direct role of this residue in the ring-opening reaction; (3) Tyr294 may also be responsible for the abstraction of the alpha-proton from d-amino acids, a prelude to the subsequent deamination reaction; (4) the steric hindrance precludes accessibility of active site functional groups to the l-amino acid substrates and may account for the stereospecificity of this enzyme toward d-amino acids. These structural data provide evidence favoring a mechanism in which the ring cleavage is induced by a nucleophilic attack at the pro-S beta-methylene carbon of ACC, with Tyr294 as the nucleophile. However, these observations are also consistent with an alternative mechanistic possibility in which the ring opening is acid-catalyzed and may be facilitated by charge relay through PLP, where Tyr294 functions as a general acid. The results of mutagenesis studies corroborated the assigned critical role for Tyr294 in the catalysis.
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(as it appears on PubMed at http://www.pubmed.gov), where 15491139 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15491139}}
==About this Structure==
==About this Structure==
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[[Category: Structure]]
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[[Category: Substrate]]
[[Category: Substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:33:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:01:35 2008''

Revision as of 00:01, 28 July 2008

Image:1tzj.png

Template:STRUCTURE 1tzj

Crystal Structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine

Template:ABSTRACT PUBMED 15491139

About this Structure

1TZJ is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5'-phosphate dependent cyclopropane ring-opening reaction., Karthikeyan S, Zhou Q, Zhao Z, Kao CL, Tao Z, Robinson H, Liu HW, Zhang H, Biochemistry. 2004 Oct 26;43(42):13328-39. PMID:15491139

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