Literature DB >> 1368511

Purification and characterization of citrate synthase from Streptomyces hygroscopicus SF-1293 and comparison of its properties with those of 2-phosphinomethylmalic acid synthase.

K W Shimotohno1, S Imai, T Murakami, H Seto.   

Abstract

To study the relationship between citrate synthase and 2-phosphinomethylmalic acid (PMM) synthase, which catalyzes a very similar reaction comparable to citrate formation in the biosynthesis of a herbicide, bialaphos, citrate synthase was purified from the mycelium of Streptomyces hygroscopicus SF-1293, a bialaphos-producing organism. The overall purification was 440-fold with a yield of 4.4% from cell-free extract. Based on comparison with PMM synthase, it has been concluded that citrate synthase of S. hygroscopicus is quite different from PMM synthase in several aspects such as enzymatic properties, amino acid composition. N-terminal amino acid sequence, and stereo-chemical reaction mechanism.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 1368511

Source DB:  PubMed          Journal:  Agric Biol Chem        ISSN: 0002-1369


  3 in total

1.  Role of acid metabolism in Streptomyces coelicolor morphological differentiation and antibiotic biosynthesis.

Authors:  P H Viollier; W Minas; G E Dale; M Folcher; C J Thompson
Journal:  J Bacteriol       Date:  2001-05       Impact factor: 3.490

2.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1991-08-25       Impact factor: 16.971

3.  Re-citrate synthase from Clostridium kluyveri is phylogenetically related to homocitrate synthase and isopropylmalate synthase rather than to Si-citrate synthase.

Authors:  Fuli Li; Christoph H Hagemeier; Henning Seedorf; Gerhard Gottschalk; Rudolf K Thauer
Journal:  J Bacteriol       Date:  2007-03-30       Impact factor: 3.490

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.