Disease relevance of ptsG

• Both genes can be stably maintained in Escherichia coli cells and restore the ability to ferment glucose to ptsG deletion mutants of E. coli [1].
• In contrast to ptsl mutants in members of the Enterobacteriaceae, the defective growth of B. subtilis ptsl mutants on glycerol was not restored by an insertion in the ptsG gene which eliminated IIGlc [2].
• Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis [3].
• The production of recombinant Rhodobacter sphaeroides aminolevulinate (ALA) synthase was optimized in two strains of Escherichia coli: the wild-type strain MG1655, and a ptsG mutant AFP111 [4].
• Comamonas testosteroni 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase (3 alpha-HSD/CR) is a key enzyme in the degradation of steroid compounds in soil and may therefore play a significant role in the bioremediation of hormonally active compounds in the environment [5].

High impact information on ptsG

• II-BGlc, a glucose receptor of the bacterial phosphotransferase system: molecular cloning of ptsG and purification of the receptor from an overproducing strain of Escherichia coli [6].
• In the present experiments, the Escherichia coli ptsG locus, which encodes II-BGlc, was isolated from a transducing phage library and subcloned into plasmid vectors [6].
• The resulting plasmids complement the following phenotypic defects of ptsG mutants: growth on glucose, uptake and phosphorylation of methyl alpha-D-glucoside, and repression of the utilization of non-PTS sugars by methyl alpha-glucoside [6].
• However, when transformed with pTSGH11 (encoding ptsG) or pAP2, this organism provided membranes that contained either the PtsG or AglA transporters, respectively [7].
• In addition, 3 alpha-HSD/CR mediates the carbonyl reduction of non-steroidal aldehydes and ketones [5].

Chemical compound and disease context of ptsG

• C-terminal fusion of a histidine hexapeptide to both gene products did not affect the activity of the enzymes and allowed their purification by Ni2+-NTA affinity chromatography after expression in a ptsG (EIICB(Glc)) deletion mutant of E. coli [8].
• Although the V. furnissii Glc-specific permease (55,941 Da) shares 38% identity with E. coli IIGlc (ptsG), it is 67% identical to MalX of the E. coli maltose operon (Reidl, J., and Boos, W. (1991) J. Bacteriol. 173, 4862-4876) [9].
• The ptsG gene of Bacillus subtilis encodes Enzyme IIGlc of the phosphoenolpyruvate: glucose phosphotransferase system [3].
• We constructed ethanologenic E. coli strains with a glucose phosphotransferase (ptsG) mutation and used the mutants to ferment glucose, arabinose, and xylose, singly and in mixtures, to ethanol [10].
• In Escherichia coli, disruption of ptsG, which encodes the glucose-specific permease of the phosphotransferase transport system (PTS) protein EIICB(Glc), is crucial for high succinate production [11].

Biological context of ptsG

• The structural gene of the permease, ptsG, has been cloned on a multicopy plasmid, and transformants constitutively overproducing the protein 10-15 times over wild-type level have been isolated [12].
• Disruption of the ptsG gene that codes for the membrane component of the major glucose transporter (IICB(Glc)), and/or the fruF gene coding for FPr (fructose-specific hybrid phosphotransferase protein), did not affect the phosphorylation state of IIA(Glc) [13].
• Genes encoding the circularly permuted precursors U(Cdelta)-IIA(Glc)-U(Ndelta) and U(Cdelta)-IICB(Glc)-U(Ndelta) were assembled from DNA fragments encoding the 3' and 5' segments of the recA intein of M. tuberculosis and crr and ptsG of E. coli, respectively [14].
• A 13-kilobase pair fragment of V. furnissii DNA was found to impart a Glc+, Man+ phenotype to Escherichia coli ptsG ptsM mutants, and encodes the mannose transporter, ptsM, of the phosphoenolpyruvate:glycose phosphotransferase system [15].
• We report here cloning of the complete ptsG gene of B. subtilis and determination of the nucleotide sequence of the 5' end [3].

Associations of ptsG with chemical compounds

• This in silico analysis predicted that disrupting the genes for three pyruvate forming enzymes, ptsG, pykF, and pykA, allows enhanced succinic acid production [16].
• The result is that ptsG expression is very similar in glucose-grown cultures of wild-type and mlc strains [17].
• Growth of B. subtilis ptsG mutants, lacking IIGlc, was not impaired on glycerol [2].
• Antibodies were generated in rabbits against the entire 3alpha-HSD/CR protein, and may now be used for evaluating the pattern of steroid induction in C. testosteroni on the protein level [18].
• The enzyme also catalyzes the carbonyl reduction of nonsteroidal aldehydes and ketones such as metyrapone, p-nitrobenzaldehyde and a novel insecticide (NKI 42255), and, based on this pluripotent substrate specificity, was named 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase (3alpha-HSD/CR) [18].

Other interactions of ptsG

• The mlc gene encodes a transcriptional regulator that has been shown to affect the expression of manXYZ and malT. ptsG mRNA levels are lower in the mlc strain grown on glucose than in the same strain grown on glycerol [17].
• A ptsG ptsM glk mutant which cannot grow on glucose can accumulate [14C]glucose via galactose permeases [19].

Analytical, diagnostic and therapeutic context of ptsG

• Upon gel permeation chromatography the purified enzyme elutes as a 49.4 kDa protein revealing for the first time the dimeric nature of 3alpha-HSD/CR of C. testosteroni [18].

References