scholarly journals The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate

1971 ◽  
Vol 123 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley
Keyword(s):  
Phosphoric Acid ◽  
Glutamic Acid ◽  
Inorganic Phosphate ◽  
Triose Phosphate Isomerase ◽  
Rabbit Muscle ◽  
Irreversible Inhibitor ◽  
Active Centre ◽  
Triose Phosphate ◽  
Glutamic Acid Residue

1. Glycidol (2,3-epoxypropanol) phosphate is a specific irreversible inhibitor of rabbit muscle triose phosphate isomerase (EC 5.3.1.1); the site of attachment has now been studied. 2. The labelled enzyme was digested with pepsin and a modified peptide isolated. The sequence of the peptide is: Ala-Tyr-Glu-Pro-Val-Trp. 3. It is the glutamic acid residue in this peptide that is labelled: the peptide is thus a γ-glutamyl ester derived from glycerol phosphoric acid. The same site is labelled by a mixture of glycidol and inorganic phosphate. 4. Kinetic and stereochemical features of these reactions are discussed.

scholarly journals Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine

1972 ◽  
Vol 129 (2) ◽  
pp. 321-331 ◽  
Author(s):  
Susan De La Mare ◽  
A. F. W. Coulson ◽  
J. R. Knowles ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Triose Phosphate Isomerase ◽  
Primary Site ◽  
Primary Proton ◽  
Carboxylate Group ◽  
Irreversible Inhibitor ◽  
Triose Phosphate ◽  
Glutamic Acid Residue ◽  
Chicken Muscle

Triose phosphate isomerase from chicken muscle reacts stoicheiometrically with the active-site-directed irreversible inhibitor bromohydroxyacetone phosphate with concomitant loss of all catalytic activity. The primary site of attachment has been shown to be a unique glutamic acid residue in the sequence Ala-Tyr-Glu-Pro-Val-Trp. Unless the inhibitor–enzyme bond is stabilized by reduction of the C-2 carbonyl group with borohydride, the phosphate group is lost and the label migrates to the adjacent tyrosine residue. It is suggested that the γ-carboxylate group of the glutamic acid residue may be the base responsible for primary proton abstraction from substrate in the catalysis. The failure of this reagent specifically to inactivate either muscle or yeast aldolase, and the use of the reagent in preparing isomerase-free glycolytic enzymes, is discussed.

scholarly journals The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase

2000 ◽  
Vol 267 (9) ◽  
pp. 2516-2524 ◽  
Author(s):  
Anne-Marie Lambeir ◽  
Jan Backmann ◽  
Javier Ruiz-Sanz ◽  
Vladimir Filimonov ◽  
Jens Erik Nielsen ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Triose Phosphate Isomerase ◽  
Leishmania Mexicana ◽  
Triose Phosphate ◽  
The Stability

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 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 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.

New inhibitors of rabbit muscle triose-phosphate isomerase

2005 ◽  
Vol 15 (11) ◽  
pp. 2906-2909 ◽  
Author(s):  
M. Fonvielle ◽  
S. Mariano ◽  
M. Therisod
Keyword(s):  
Triose Phosphate Isomerase ◽  
Rabbit Muscle ◽  
Triose Phosphate

scholarly journals The active centre of triose phosphate isomerase

1966 ◽  
Vol 100 (3) ◽  
pp. 702-710 ◽  
Author(s):  
PM Burton ◽  
SG Waley
Keyword(s):  
Triose Phosphate Isomerase ◽  
Active Centre ◽  
Triose Phosphate
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