Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin

Price, Nicholas C.; Duncan, David S.; McAlister, J W

doi:10.1042/bj2290167

Cited by 21 publications

(12 citation statements)

References 21 publications

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“…The C-terminal tail is particularly susceptible to proteolysis, and a phosphoglycerate mutase molecule which has lost these residues, but is otherwise apparently unmodified shows complete loss of mutase activity. These observations have been noted for both the yeast enzyme (Sasaki et al, 1966;Winn et al, 1981) and the rabbit muscle enzyme (Price et al, 1985b). The proteolyzed yeast mutase retains phosphatase activity toward 2,3-bisphosphoglycerate and can thus still bind the bisphospho ligand.…”

Section: C-terminal Tailmentioning

confidence: 61%

The Phosphoglycerate Mutases

Fothergill‐Gilmore

Watson

1989

Advances in Enzymology - And Related Areas of Molecular Biology

131

100

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Section: C-terminal Tailmentioning

confidence: 61%

The Phosphoglycerate Mutases

Fothergill‐Gilmore

Watson

1989

Advances in Enzymology - And Related Areas of Molecular Biology

131

100

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“…4(a). There is no significant further change in the spectrum when the concentration of GdnHCl is raised to 4 M. The spectra can be compared with those previously published for the baker's yeast and rabbit muscle enzymes (Hermann et al, 1983;Price et al, 1985b By the analysis of Siegel et al (1980), which depends on the values of 0 over a range of wavelengths from 210 to 240 nm, the percentage of helical structure can be estimated as 27.9 + 1.6, 39.8 + 1.6 (S. pombe dialysed and undialysed respectively), 12.2+1.9 (baker's yeast) and 9.7 + 2 (rabbit muscle). It should be noted that the percentage helical structure for the baker's-yeast enzyme derived from c.d.…”

Section: Stability Of S Pombe Phosphoglycerate Mutasementioning

confidence: 99%

“…In previous work with the rabbit muscle enzyme (Price et al, 1985b) it was also found that the phosphorylated form of the enzyme was less susceptible to proteolysis by thermolysin than the dephosphoenzyme. is a small (< 15%) but reproducible increase in activity at concentrations of GdnHCl up to 0.5 M, followed by a sharp decline in the range 0.5-1.5 M, with 50% activity lost at 0.85 M-GdnHCl.…”

Section: Stability Of S Pombe Phosphoglycerate Mutasementioning

confidence: 99%

Denaturation and renaturation of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe

Johnson

Price

1987

Biochemical Journal

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The denaturation by guanidinium chloride of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe was studied. The loss in activity broadly parallels the changes in protein structure detected by fluorescence and c.d. Renaturation can be brought about by dilution of the denaturing agent. These processes were compared with those in the enzymes from baker's yeast and rabbit muscle, which are tetrameric and dimeric respectively. The effects of the cofactor 2,3-bisphosphoglycerate on the structure and stability of the S. pombe enzyme were also investigated.

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“…The lack of or relatively low PGM activity of YhfR is somewhat surprising, given the sequence homology of this protein with dPGMs including the enzyme from S. cerevisiae noted above. However, the yeast enzyme has 36 internal residues not present in YhfR, and the sequences in the carboxy-terminal regions of the two proteins are very different; there are also a variety of data indicating that the carboxy-terminal regions of dPGMs are important for enzyme function (18,24,25,27). In addition, comparison of putative dPGM sequences from Bacillus stearothermophilus, B. subtilis, Clostridium acetobutylicum, and Clostridium difficile, all of which are spore formers, showed a surprising lack of sequence conservation, with only ϳ13% identical residues in the proteins from these four species (data not shown).…”

mentioning

confidence: 99%

Analysis of the Function of a Putative 2,3-Diphosphoglyceric Acid-Dependent Phosphoglycerate Mutase from Bacillus subtilis

et al. 2000

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A Bacillus subtilis gene termed yhfR encodes the only B. subtilis protein with significant sequence similarity to 2,3-diphosphoglycerate-dependent phosphoglycerate mutases (dPGM). This gene is expressed at a low level during growth and sporulation, but deletion of yhfR had no effect on growth, sporulation, or spore germination and outgrowth. YhfR was expressed in and partially purified from Escherichia coli but had little if any PGM activity and gave no detectable PGM activity in B. subtilis. These data indicate that B. subtilis does not require YhfR and most likely does not require a dPGM.Phosphoglycerate mutase (PGM) catalyzes the interconversion of 3-phosphoglyceric acid (3PGA) and 2PGA in both glycolysis and gluconeogenesis. Two types of PGM have been identified; one is dependent on 2,3-diphosphoglycerate (DPG) for activity (dPGM), and the other is not (iPGM) (5, 6). These two types of PGM differ strikingly in their structures, mechanisms, and amino acid sequences (3,5,6,8,9,10). Some organisms appear to contain only a single type of PGM, while others contain both types of PGM (2,5,6,7). Among the latter is Escherichia coli, which contains genes for both an iPGM and a dPGM; both genes are expressed at somewhat similar levels, and both give functional enzymes (7).In Bacillus subtilis the great majority (Ն90%) of PGM activity is due to an iPGM (20,26), and mutation of the coding gene (termed pgm) has very severe effects on cell growth, especially in the presence of glucose (13). Although this iPGM appears to be the major PGM in B. subtilis, determination of the complete sequence of the B. subtilis genome revealed only a single gene, termed yhfR, that codes for a protein with significant sequence similarity to dPGMs (11), (see below). This raised the possibility that, like E. coli, B. subtilis also might contain two types of PGM under some conditions. In order to probe the possible function of yhfR in B. subtilis, we first determined if this gene was expressed at any significant level by construction and analysis of the expression of translational yhfR-lacZ fusions. A fragment from 191 bp upstream of to 28 bp into the yhfR coding sequence was amplified by PCR; the primers used contained extra residues with either BamHI or EcoRI sites at their 5Ј ends. The 226-bp PCR product was cut with BamHI and EcoRI and cloned between these sites in plasmid pJF751, a vector for construction of translational lacZ fusions (4), giving plasmid pPS3083. This plasmid was sequenced to confirm the expected DNA sequence in the yhfRlacZ region and then used to transform our wild-type B. subtilis 168 strain (PS832) to chloramphenicol resistance (Cm r ) by integration at the yhfR locus through a single-crossover event. Southern blot analysis confirmed that the resultant strain (PS3113) contained a single copy of the yhfR-lacZ fusion at yhfR. To insert the translational yhfR-lacZ fusion at the amyE locus, plasmid pPS3083 was digested with EcoRI and ClaI and the resulting fragment carrying the lacZ fusion was cloned between the EcoRI and ...

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Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin

Cited by 21 publications

References 21 publications

The Phosphoglycerate Mutases

The Phosphoglycerate Mutases

Denaturation and renaturation of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe

Analysis of the Function of a Putative 2,3-Diphosphoglyceric Acid-Dependent Phosphoglycerate Mutase from Bacillus subtilis

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