Literature DB >> 9573215

Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis.

S Schönert1, T Buder, M K Dahl.   

Abstract

A gene coding for a putative alpha-glucosidase has been identified in the open reading frame yvdL (now termed malL), which was sequenced as part of the Bacillus subtilis genome project. The enzyme was overproduced in Escherichia coli and purified. Further analyses indicate that MalL is a specific oligo-1,4-1,6-alpha-glucosidase (sucrase-maltase-isomaltase). MalL expression in B. subtilis requires maltose induction and is subject to carbon catabolite repression by glucose and fructose. Insertional mutagenesis of malL resulted in a complete inactivation of the maltose-inducible alpha-glucosidase activity in crude protein extracts and a Mal- phenotype.

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Year:  1998        PMID: 9573215      PMCID: PMC107205          DOI: 10.1128/JB.180.9.2574-2578.1998

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  26 in total

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  18 in total

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Authors:  H Yamamoto; M Serizawa; J Thompson; J Sekiguchi
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4.  Maltose and maltodextrin utilization by Bacillus subtilis.

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6.  The glucose kinase of Bacillus subtilis.

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7.  Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.

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8.  Molecular and functional characterization of a unique sucrose hydrolase from Xanthomonas axonopodis pv. glycines.

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9.  Isomaltose production by modification of the fructose-binding site on the basis of the predicted structure of sucrose isomerase from "Protaminobacter rubrum".

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Journal:  J Bacteriol       Date:  2009-05-22       Impact factor: 3.490

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