2reh

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{{STRUCTURE_2reh| PDB=2reh | SCENE= }}
{{STRUCTURE_2reh| PDB=2reh | SCENE= }}
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'''Mechanistic and Structural Analyses of the Roles of Arg409 and Asp402 in the Reaction of the Flavoprotein Nitroalkane Oxidase'''
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===Mechanistic and Structural Analyses of the Roles of Arg409 and Asp402 in the Reaction of the Flavoprotein Nitroalkane Oxidase===
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==Overview==
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The flavoprotein nitroalkane oxidase (NAO) catalyzes the oxidation of primary and secondary nitroalkanes to the corresponding aldehydes and ketones. The enzyme is a homologue of acyl-CoA dehydrogenase. Asp402 in NAO has been proposed to be the active site base responsible for removing the substrate proton in the first catalytic step; structurally it corresponds to the glutamate which acts as the base in medium chain acyl-CoA dehydrogenase. In the active site of NAO, the carboxylate of Asp402 forms an ionic interaction with the side chain of Arg409. The R409K enzyme has now been characterized kinetically and structurally. The mutation results in a decrease in the rate constant for proton abstraction of 100-fold. Analysis of the three-dimensional structure of the R409K enzyme, determined by X-ray crystallography to a resolution of 2.65 A, shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409. The D402E mutation results in a smaller decrease in the rate constant for proton abstraction of 18-fold. The structure of the D402E enzyme, determined at 2.4 A resolution, shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402, and the interaction of this residue with Ser276 is perturbed. These results establish the critical importance of the interaction between Asp402 and Arg409 for proton abstraction by nitroalkane oxidase.
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{{ABSTRACT_PUBMED_17994768}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase., Fitzpatrick PF, Bozinovski DM, Heroux A, Shaw PG, Valley MP, Orville AM, Biochemistry. 2007 Dec 4;46(48):13800-8. Epub 2007 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17994768 17994768]
Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase., Fitzpatrick PF, Bozinovski DM, Heroux A, Shaw PG, Valley MP, Orville AM, Biochemistry. 2007 Dec 4;46(48):13800-8. Epub 2007 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17994768 17994768]
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Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover., Nagpal A, Valley MP, Fitzpatrick PF, Orville AM, Biochemistry. 2006 Jan 31;45(4):1138-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16430210 16430210]
[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
[[Category: Nitroalkane oxidase]]
[[Category: Nitroalkane oxidase]]
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[[Category: Nitroalkanefad]]
[[Category: Nitroalkanefad]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:52:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:25:13 2008''

Revision as of 10:25, 28 July 2008

Image:2reh.png

Template:STRUCTURE 2reh

Mechanistic and Structural Analyses of the Roles of Arg409 and Asp402 in the Reaction of the Flavoprotein Nitroalkane Oxidase

Template:ABSTRACT PUBMED 17994768

About this Structure

2REH is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

Reference

Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase., Fitzpatrick PF, Bozinovski DM, Heroux A, Shaw PG, Valley MP, Orville AM, Biochemistry. 2007 Dec 4;46(48):13800-8. Epub 2007 Nov 10. PMID:17994768

Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover., Nagpal A, Valley MP, Fitzpatrick PF, Orville AM, Biochemistry. 2006 Jan 31;45(4):1138-50. PMID:16430210

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