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1w9x

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==Overview==
==Overview==
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The enzymatic digestion of starch by alpha-amylases is one of the key, biotechnological reactions of recent times. In the search for industrial, biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus, has been cloned and expressed. The three-dimensional structure at 2.1 A, resolution has been determined in complex with the (pseudo)tetrasaccharide, inhibitor acarbose. Acarbose is found bound as a nonasaccharide, transglycosylation product spanning the -6 to +3 subsites. Careful, inspection of electron density suggests that the bound ligand could not, have been formed through successive transglycosylations of acarbose and, must also have featured maltose or maltooligosaccharides as an acceptor.
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The enzymatic digestion of starch by alpha-amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus has been cloned and expressed. The three-dimensional structure at 2.1 A resolution has been determined in complex with the (pseudo)tetrasaccharide inhibitor acarbose. Acarbose is found bound as a nonasaccharide transglycosylation product spanning the -6 to +3 subsites. Careful inspection of electron density suggests that the bound ligand could not have been formed through successive transglycosylations of acarbose and must also have featured maltose or maltooligosaccharides as an acceptor.
==About this Structure==
==About this Structure==
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[[Category: Bacillus halmapalus]]
[[Category: Bacillus halmapalus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Borchert, T.V.]]
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[[Category: Borchert, T V.]]
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[[Category: Brzozowski, A.M.]]
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[[Category: Brzozowski, A M.]]
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
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[[Category: Davies, G.J.]]
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[[Category: Davies, G J.]]
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[[Category: Rasmussen, M.D.]]
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[[Category: Rasmussen, M D.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: NA]]
[[Category: NA]]
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[[Category: glycoside hydrolase]]
[[Category: glycoside hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:21:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:01 2008''

Revision as of 13:42, 21 February 2008


1w9x, resolution 2.10Å

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BACILLUS HALMAPALUS ALPHA AMYLASE

Overview

The enzymatic digestion of starch by alpha-amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus has been cloned and expressed. The three-dimensional structure at 2.1 A resolution has been determined in complex with the (pseudo)tetrasaccharide inhibitor acarbose. Acarbose is found bound as a nonasaccharide transglycosylation product spanning the -6 to +3 subsites. Careful inspection of electron density suggests that the bound ligand could not have been formed through successive transglycosylations of acarbose and must also have featured maltose or maltooligosaccharides as an acceptor.

About this Structure

1W9X is a Single protein structure of sequence from Bacillus halmapalus with and as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution., Davies GJ, Brzozowski AM, Dauter Z, Rasmussen MD, Borchert TV, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):190-3. Epub 2005, Jan 19. PMID:15681870

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