Carbohydrate transport in bacteria

Dills, S S; Apperson, A; Schmidt, Mary R.; Saier, Milton H.

doi:10.1128/mr.44.3.385-418.1980

Cited by 197 publications

(12 citation statements)

References 203 publications

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“…aureus by group translocation, may also be sensitive to pH (Reider et al, 1979;Dills et al, 1980;Robillard & Konings, 1981). The initial rate of glycolysis in S. aureus in the presence of octanoate is slightly less than that of the control cells; however, metabolic activity ceases midway during glycolysis (see Results).…”

Section: Discussionmentioning

confidence: 87%

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Ezra¹,

Lucas²,

Mustacich³

et al. 1983

Biochemistry

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Section: Discussionmentioning

confidence: 87%

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Ezra¹,

Lucas²,

Mustacich³

et al. 1983

Biochemistry

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“…e phosphoenolpyruvate (PEP)'-dependent protein kinase enzyme I is part of the PEP-dependent phosphotransferase system (PTS) which catalyzes carbohydrate uptake in microorganisms (Hengstenberg, 1977;Dills et al, 1980;Robillard, 1982).…”

mentioning

confidence: 99%

Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center

Alpert¹,

Frank²,

Stueber³

et al. 1985

Biochemistry

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Enzyme I, the phosphoenolpyruvate:protein phosphotransferase (EC 2.7.3.9), which is part of the bacterial phosphoenolpyruvate- (PEP) dependent phosphotransferase system, has been purified from Streptococcus faecalis by using a large-scale preparation. Size exclusion chromatography revealed a molecular weight of 140 000. On sodium dodecyl sulfate gels, enzyme I gave one band with a molecular weight of 70 000, indicating that enzyme I consists of two identical subunits. The first 59 amino acids of the amino-terminal part of the protein have been sequenced. It showed some similarities with enzyme I of Salmonella typhimurium. The active center of enzyme I has also been determined. After phosphorylation with [32P]PEP, the enzyme was cleaved by using different proteases. Labeled peptides were isolated by high-performance liquid chromatography on a reversed-phase column. The amino acid composition or amino acid sequence of the peptides has been determined. The largest labeled peptide was obtained with Lys-C protease and had the following sequence: -Ala-Phe-Val-Thr-Asp-Ile-Gly- Gly-Arg-Thr-Ser-His*-Ser-Ala-Ile-Met-Ala-Arg-Ser-Leu-Glu-Ile-Pro-Ala- Ile-Val-Gly-Thr-Lys-. It has previously been shown that the phosphoryl group is bound to the N-3 position of a histidyl residue in phosphorylated enzyme I. The single His in position 12 of the above peptide must therefore carry the phosphoryl group.

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“…In the NMR spectrum the labeling of the arginyl residue influences the resonance lines of His-15: two new resonance lines for the C-2 protons of equal intensity are observed, a fact that could be explained by two different conformations in slow exchange. The pK value of His-15 was not changed by the labeling, excluding Arg-17 as responsible for the low pK of Ilpr1 is a constitutive protein of the phosphoenolpyruvate-dependent phosphotransferase system (PTS), a carbohydrate transport system found in virtually all anaerobic and facultatively anaerobic bacteria [for a review see, e.g., Hengstenberg (1977), Dills et al (1980), or Robillard (1982)].…”

mentioning

confidence: 99%

Phosphoenolpyruvate-dependent phosphotransferase system. Proton NMR studies on chemically modified heat-stable proteins

Kalbitzer¹,

Muss²,

Engelmann³

et al. 1985

Biochemistry

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The low-pK tyrosyl residue present in the heat-stable proteins (HPr) of all Gram-positive bacteria studied until now has been labeled by tetranitromethane in the HPr of Bacillus subtilis and Streptococcus faecalis. The nitrotyrosyl derivatives obtained are fully active in the complementation assay. The labeled tyrosyl residues could be identified as Tyr-37 in both proteins. Reinvestigation of the low-pK tyrosyl residue in HPr of Staphylococcus aureus resulted in the same assignment. In all three proteins an interaction between nitrotyrosine-37 and the active center His-15 could be observed, leading to an increase in the pK of His-15 and a change of its chemical shift parameters. The 1H NMR lines of the complete aromatic spin system of HPr of B. subtilis could be assigned by the nitration studies. Labeling of Arg-17 in HPr of S. aureus and S. faecalis by 1,2-cyclohexanedione in the presence of borate ions causes an almost complete inhibition of its enzymatic activity. In the NMR spectrum the labeling of the arginyl residue influences the resonance lines of His-15: two new resonance lines for the C-2 protons of equal intensity are observed, a fact that could be explained by two different conformations in slow exchange. The pK value of His-15 was not changed by the labeling, excluding Arg-17 as responsible for the low pK of His-15.

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Carbohydrate transport in bacteria

Cited by 197 publications

References 203 publications

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Phosphorus-31 and carbon-13 nuclear magnetic resonance studies of anaerobic glucose metabolism and lactate transport in Staphylococcus aureus cells

Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center

Phosphoenolpyruvate-dependent phosphotransferase system. Proton NMR studies on chemically modified heat-stable proteins

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