Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Eschirichia coli
Article Abstract:
A gene cluster in the Escherichia coli chromosome's 67.4-76.0 min region was revealed via systematic genome sequencing. Five genes encode homologues of the phosphotransferase system's mannose permease. Other genes encode a putative N-acetylgalactosamine 6-phosphate metabolic pathway that includes a deacetylase, an aldolase, a putative carbohydrate kinase and an isomerizing deaminase. A transcriptional regulatory protein is homologous to DeoR family members. Results suggest that the aldolase-encoding gene found in the cluster is the previously designated kba gene that encodes tagatose-1,6-biphosphate aldolase.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Identification and characterization of phosphoenolpyruvate:fructose phosphotransferase systems in three Streptomyces species
Article Abstract:
A study of three Streptomyces species, Streptomyces coelicolor, Streptomyces lividans and Streptomyces griseofuseus, for the presence of components of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) reveals that Enzyme I, fructose-specific Enzyme II and HPr are present in all three species. S. griseofuseus exhibits the constitutive expression of PTS enzymes, while in S. coelicolor and S. lividans the enzymes are induced by fructose. The low-GC gram-positive bacteria-specific HPr (Ser-P) phosphatase and HPr (Ser) kinase are absent in all three species.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Novel phosphotransferase system genes revealed by bacterial genome analysis - a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system
Article Abstract:
The genomic sequencing of the Escherichia coli genome revealed a gene phosphoenolpyruvate:sugar phosphotransferase system (ptsA) that encodes a new Enzyme I homologue in the 89.1-89.3 centisome region. Analysis provided the following characteristics of the region: open reading frames (ORFs) that encode a fused PTS Enzyme I-IIAfru homologue, a glycerol dehydrogenase, a transaldolase homologue, two PTS IIBfru homologues, and homologues of pyruvate formate-lyase and its activating enzyme. Some of the proteins identified might function in anaerobic carbon metabolism.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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