Literature DB >> 23194588

The catabolism of 3-ketolactose in Agrobacterium.

D Janssens1, K Kersters, J De Ley.   

Abstract

The existence of a novel enzyme, catalyzing the hydrolysis of 3-ketolactose, is described in the different genetic groups of the genus Agrobacterium. The enzyme differs from the other glycosidases formed by Agrobacterium during growth on lactose. The inducibility of the enzyme could be demonstrated in a strain from biotype 1, but not in a strain from biotype 2. The specific activity of the 3-ketolactose hydrolase is higher in extracts of strains belonging to biotype 2 than to biotype 1. The optimum pH of the enzyme in Tris-HCl buffer is 8.4-8.5. The K(m) value for 3-ketolactose is 2.2 × 10(-2) M. The 3-ketolactose hydrolase is stimulated by Mg(2+) and Mn(2+), and inhibited by Zn(2+). Mercaptoethanol promotes the reaction rate in extracts of strains of biotype 1 but not in extracts of strains of bio-type 2.
Copyright © 1983 Gustav Fischer Verlag, Stuttgart/New York. Published by Elsevier GmbH.. All rights reserved.

Entities:  

Year:  1983        PMID: 23194588     DOI: 10.1016/S0723-2020(83)80045-9

Source DB:  PubMed          Journal:  Syst Appl Microbiol        ISSN: 0723-2020            Impact factor:   4.022


  3 in total

1.  The effect of pH and oxygen concentration on the formation of 3-ketodisaccharides by Agrobacterium tumefaciens.

Authors:  E Stoppok; J Walter; K Buchholz
Journal:  Appl Microbiol Biotechnol       Date:  1995 Aug-Sep       Impact factor: 4.813

2.  Agrobacterium vitis nopaline Ti plasmid pTiAB4: relationship to other Ti plasmids and T-DNA structure.

Authors:  L Otten; P De Ruffray
Journal:  Mol Gen Genet       Date:  1994-11-15

3.  Filling gaps in bacterial catabolic pathways with computation and high-throughput genetics.

Authors:  Morgan N Price; Adam M Deutschbauer; Adam P Arkin
Journal:  PLoS Genet       Date:  2022-04-13       Impact factor: 5.917

  3 in total

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