scholarly journals Inhibition of glycolytic enzymes by 2-phosphotartronate

1976 ◽  
Vol 153 (3) ◽  
pp. 741-744 ◽  
Author(s):  
M K Thomas ◽  
T G Spring
Keyword(s):  
Pyruvate Kinase ◽  
Competitive Inhibition ◽  
Phosphoglycerate Kinase ◽  
Triose Phosphate Isomerase ◽  
Glycolytic Enzymes ◽  
Phosphoglycerate Mutase ◽  
Rabbit Muscle ◽  
Triose Phosphate ◽  
Permanganate Oxidation

2-Phosphotartronate has been synthesized by permanganate oxidation of glycerol 2-phosphate and has been tested as an inhibitor of five glycolytic enzymes that bind phosphoglycerate or phosphoglycollate. Competitive inhibition of rabbit muscle phosphoglycerate mutase, enolase and pyruvate kinase was observed. Triose phosphate isomerase and 3-phosphoglycerate kinase were not inhibited.

scholarly journals Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase

1986 ◽  
Vol 238 (1) ◽  
pp. 275-281 ◽  
Author(s):  
A Pawluk ◽  
R K Scopes ◽  
K Griffiths-Smith
Keyword(s):  
Pyruvate Kinase ◽  
Zymomonas Mobilis ◽  
Specific Activity ◽  
High Specific Activity ◽  
Phosphoglycerate Kinase ◽  
Glycolytic Enzymes ◽  
Phosphoglycerate Mutase ◽  
Eukaryotic Species ◽  
Sugar Phosphates ◽  
Subunit Size

The five glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and pyruvate kinase were each purified from extracts of Zymomonas mobilis cells, by using dye-ligand chromatography as the principal step. Two procedures, producing three and two of the enzymes respectively, are described in detail. Z. mobilis glyceraldehyde-phosphate dehydrogenase was found to be similar in most respects to the enzyme from other sources, except for having a slightly larger subunit size. Phosphoglycerate kinase has properties typical for this enzyme; however, it did not show the sulphate activation effects characteristic of this enzyme from most other sources. Phosphoglycerate mutase is a dimer, partially independent of 2,3-bisphosphoglycerate, and has a high specific activity. Enolase was found to be octameric; otherwise its properties were very similar to those of the yeast enzyme. Pyruvate kinase is unusual in being dimeric, and not requiring K+ for activity. It is not allosterically activated by sugar phosphates, having a high activity in the absence of any effectors. Some quantitative differences in the relative amounts of these enzymes, compared with eukaryotic species, are ascribed to the fact that Z. mobilis utilizes the Entner-Doudoroff pathway rather than the more common Embden-Meyerhoff glycolytic route.

Chemistry of proton abstraction by glycolytic enzymes (aldolase, isomerases and pyruvate kinase)

1981 ◽  
Vol 293 (1063) ◽  
pp. 131-143 ◽  
Keyword(s):  
Proton Transfer ◽  
Pyruvate Kinase ◽  
Triose Phosphate Isomerase ◽  
Transfer Mechanism ◽  
Glycolytic Enzymes ◽  
Structural Homology ◽  
Large Measure ◽  
Proton Abstraction ◽  
Triose Phosphate

Intermediates have been synthesized that are rapidly utilized by triose phosphate isomerase, yeast aldolase and pyruvate kinase. In each case the compounds have the properties of an enol expected for a stepwise proton transfer mechanism. Apparently the apparatus required for doing this chemistry is sufficiently unique for a large measure of structural homology to have been imposed upon the enzymes of this class during evolution.

scholarly journals Phosphonomethyl analogues of phosphate ester glycolytic intermediates

1974 ◽  
Vol 141 (3) ◽  
pp. 715-719 ◽  
Author(s):  
Henry B. F. Dixon ◽  
Michael J. Sparkes
Keyword(s):  
Phosphoglycerate Kinase ◽  
Triose Phosphate Isomerase ◽  
Glycolytic Enzymes ◽  
Phosphate Group ◽  
Phosphate Ester ◽  
Dihydroxyacetone Phosphate ◽  
Triose Phosphate ◽  
Glycolytic Intermediates ◽  
Combined Action ◽  
Made In

Analogues of dihydroxyacetone phosphate and of 3-phosphoglycerate were made in which the phosphate group, –O–PO3H2, is replaced by the phosphonomethyl group, –CH2–PO3H2. The analogue of dihydroxyacetone phosphate is a substrate for aldolase and glycerol 1-phosphate dehydrogenase (Stribling, 1974), but not for triose phosphate isomerase. The analogue of 3-phosphoglycerate oxidizes NADH under the combined action of 3-phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase if ATP is added. Thus four out of the five glycolytic enzymes tested handle the phosphonomethyl compounds like the natural phosphates.

scholarly journals Studies of triose phosphate isomerase by hydrogen exchange

1974 ◽  
Vol 141 (3) ◽  
pp. 753-760 ◽  
Author(s):  
Christopher A. Browne ◽  
Stephen G. Waley
Keyword(s):  
Hydrogen Exchange ◽  
Marked Effect ◽  
Protein Analysis ◽  
Hollow Fibre ◽  
Triose Phosphate Isomerase ◽  
Rabbit Muscle ◽  
Structural Rearrangements ◽  
Triose Phosphate ◽  
Chicken Muscle ◽  
Low Concentrations

The3H–H exchange of chicken muscle and rabbit muscle triose phosphate isomerases was studied. Their behaviour was mostly very similar. ‘Exchange-in’ (acquisition of radioactivity when protein was incubated in3H2O) was measured at 37°C and at pH7.5, and the rates of exchange of the native and liganded enzymes were compared. Inhibitors and substrates retarded exchange, substrates showing the most marked effect; structural rearrangements in the enzyme may thus play some part in catalysis. The inhibitor phosphoglycollate affected the rabbit enzyme, but had little or no effect on the chicken enzyme. ‘Exchange-out’ (loss of radioactivity from protein previously labelled by incubation in3H2O) was measured by hollow-fibre dialysis. When ligand was removed during the course of dialysis (by replacing buffer that contained ligand with buffer that lacked ligand) there was a prompt decrease in the number of labelled H atoms of the protein. Analysis of the curves provides some information about the number and half-lives of the responsive H atoms. Ligands decrease the motility of the protein and affect about one-fifth of the chain. Low concentrations of glycerol 3-phosphate have an effect that is greater than expected.

scholarly journals Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase

1971 ◽  
Vol 122 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley
Keyword(s):  
Amino Acid ◽  
Cyanogen Bromide ◽  
Triose Phosphate Isomerase ◽  
Amino Acid Sequences ◽  
Cysteine Residues ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Triose Phosphate ◽  
Methionine Residues ◽  
Polypeptide Chains

1. The nature of the subunits in rabbit muscle triose phosphate isomerase has been investigated. 2. Amino acid analyses show that there are five cysteine residues and two methionine residues/subunit. 3. The amino acid sequences around the cysteine residues have been determined; these account for about 75 residues. 4. Cleavage at the methionine residues with cyanogen bromide gave three fragments. 5. These results show that the subunits correspond to polypeptide chains, containing about 230 amino acid residues. The chains in triose phosphate isomerase seem to be shorter than those of other glycolytic enzymes.

scholarly journals The tryptic peptides of rabbit muscle triose phosphate isomerase

1974 ◽  
Vol 139 (1) ◽  
pp. 1-10 ◽  
Author(s):  
P. H. Corran ◽  
S. G. Waley
Keyword(s):  
Gel Filtration ◽  
Paper Electrophoresis ◽  
Triose Phosphate Isomerase ◽  
British Library ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Tryptic Peptides ◽  
Triose Phosphate ◽  
Lending Library ◽  
Polypeptide Chains

1. The peptides obtained by tryptic digestion of S-[14C]carboxymethylated rabbit muscle triose phosphate isomerase have been studied. 2. The first step in the fractionation of the tryptic digest was gel filtration on coupled columns of Sephadex G-25 and G-50. Further fractionation was carried out by paper electrophoresis and paper chromatography. 3. The digest contained 26 peptides and three free amino acids. The sizes of the peptides ranged from two to 29 residues. 4. The sequences of the peptides have been determined. 5. The length of the polypeptide chains is about 250 amino acid residues. 6. The variant sequences encountered were due to partial deamidation; this may be one of the reasons for multiple forms of the enzyme. 7. The chicken and rabbit enzymes are compared. 8. Detailed evidence for the sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50024 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1973) 131, 5.

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