Document Detail


A novel catalytic ability of gamma-glutamylcysteine synthetase of Escherichia coli and its application in theanine production.
MedLine Citation:
PMID:  19966457     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Gamma-glutamylcysteine synthetase (gammaGCS, EC 6.3.2.2) catalyzes the formation of gamma-glutamylcysteine from L-glutamic acid (Glu) and L-cysteine (Cys) in an ATP-dependent manner. While gammaGCS can use various amino acids as substrate, little is known about whether it can use non-amino acid compounds in place of Cys. We determined that gammaGCS from Escherichia coli has the ability to combine Glu and amines to form gamma-glutamylamides. The reaction rate depended on the length of the methylene chain of the amines in the following order: n-propylamine > butylamine > ethylamine >> methylamine. The optimal pH for the reaction was narrower and more alkaline than for the reaction with an amino acid. The newly found catalytic ability of gammaGCS was used in the production of theanine (gamma-glutamylethylamine). The resting cells of E. coli expressing gammaGCS, in which ATP was regenerated through glycolysis, synthesized 12.1 mM theanine (18 h) from 429 mM ethylamine.
Authors:
Koichiro Miyake; Shingo Kakita
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Publication Detail:
Type:  Journal Article     Date:  2009-12-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  73     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-12-24     Completed Date:  2010-03-08     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2677-83     Citation Subset:  IM    
Affiliation:
Technical Research Laboratories, Kyowa Hakko Bio Co., Ltd., Hofu, Yamaguchi, Japan. koichiro.miyake@kyowa-kirin.co.jp
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MeSH Terms
Descriptor/Qualifier:
Biocatalysis*
Escherichia coli / cytology,  enzymology*,  genetics,  metabolism
Ethylamines / metabolism
Glutamate-Cysteine Ligase / biosynthesis,  isolation & purification,  metabolism*
Glutamates / biosynthesis*
Hydrogen-Ion Concentration
Substrate Specificity
Chemical
Reg. No./Substance:
0/Ethylamines; 0/Glutamates; 3081-61-6/theanine; 75-04-7/ethylamine; EC 6.3.2.2/Glutamate-Cysteine Ligase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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