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4gyl

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{{STRUCTURE_4gyl| PDB=4gyl | SCENE= }}
{{STRUCTURE_4gyl| PDB=4gyl | SCENE= }}
===The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine===
===The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine===
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{{ABSTRACT_PUBMED_23946488}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
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[[4gyl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYL OCA].
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[[4gyl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsp Bacsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYL OCA].
==Reference==
==Reference==
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<references group="xtra"/><references/>
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<ref group="xtra">PMID:023946488</ref><references group="xtra"/><references/>
[[Category: Amidase]]
[[Category: Amidase]]
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[[Category: Bacillus sp.]]
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[[Category: Bacsp]]
[[Category: Cowan, D A.]]
[[Category: Cowan, D A.]]
[[Category: Hunter, R.]]
[[Category: Hunter, R.]]

Revision as of 08:26, 5 February 2014

Template:STRUCTURE 4gyl

Contents

The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine

Template:ABSTRACT PUBMED 23946488

Function

[AMIE_BACSP] Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia.[1] Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates (By similarity).[2]

About this Structure

4gyl is a 1 chain structure with sequence from Bacsp. Full crystallographic information is available from OCA.

Reference

  • Weber BW, Kimani SW, Varsani A, Cowan DA, Hunter R, Venter GA, Gumbart JC, Sewell BT. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J Biol Chem. 2013 Oct 4;288(40):28514-23. doi: 10.1074/jbc.M113.503284. Epub 2013, Aug 14. PMID:23946488 doi:http://dx.doi.org/10.1074/jbc.M113.503284
  1. ↑ Kim S, Oriel P. Cloning and expression of the nitrile hydratase and amidase genes from Bacillus sp. BR449 into Escherichia coli. Enzyme Microb Technol. 2000 Oct 1;27(7):492-501. PMID:10978771
  2. ↑ Kim S, Oriel P. Cloning and expression of the nitrile hydratase and amidase genes from Bacillus sp. BR449 into Escherichia coli. Enzyme Microb Technol. 2000 Oct 1;27(7):492-501. PMID:10978771

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