1q6d: Difference between revisions

Revision as of 23:59, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q6d.png

Template:STRUCTURE 1q6d

Crystal structure of Soybean Beta-Amylase Mutant (M51T) with Increased pH OptimumCrystal structure of Soybean Beta-Amylase Mutant (M51T) with Increased pH Optimum

Template:ABSTRACT PUBMED 14638688

About this StructureAbout this Structure

1Q6D is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum., Hirata A, Adachi M, Sekine A, Kang YN, Utsumi S, Mikami B, J Biol Chem. 2004 Feb 20;279(8):7287-95. Epub 2003 Nov 24. PMID:14638688

Page seeded by OCA on Sun Jul 27 23:59:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1q6d.gif|left|200px]]
+{{Seed}}
+[[Image:1q6d.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1q6d|  PDB=1q6d  |  SCENE=  }}
-'''Crystal structure of Soybean Beta-Amylase Mutant (M51T) with Increased pH Optimum'''
+===Crystal structure of Soybean Beta-Amylase Mutant (M51T) with Increased pH Optimum===
-==Overview==
+<!--
-Comparison of the architecture around the active site of soybean beta-amylase and Bacillus cereus beta-amylase showed that the hydrogen bond networks (Glu380-(Lys295-Met51) and Glu380-Asn340-Glu178) in soybean beta-amylase around the base catalytic residue, Glu380, seem to contribute to the lower pH optimum of soybean beta-amylase. To convert the pH optimum of soybean beta-amylase (pH 5.4) to that of the bacterial type enzyme (pH 6.7), three mutants of soybean beta-amylase, M51T, E178Y, and N340T, were constructed such that the hydrogen bond networks were removed by site-directed mutagenesis. The kinetic analysis showed that the pH optimum of all mutants shifted dramatically to a neutral pH (range, from 5.4 to 6.0-6.6). The Km values of the mutants were almost the same as that of soybean beta-amylase except in the case of M51T, while the Vmax values of all mutants were low compared with that of soybean beta-amylase. The crystal structure analysis of the wild type-maltose and mutant-maltose complexes showed that the direct hydrogen bond between Glu380 and Asn340 was completely disrupted in the mutants M51T, E178Y, and N340T. In the case of M51T, the hydrogen bond between Glu380 and Lys295 was also disrupted. These results indicated that the reduced pKa value of Glu380 is stabilized by the hydrogen bond network and is responsible for the lower pH optimum of soybean beta-amylase compared with that of the bacterial beta-amylase.
+The line below this paragraph, {{ABSTRACT_PUBMED_14638688}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14638688 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14638688}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Increased ph optimum]]
 [[Category: Maltose complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:55:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:59:33 2008''