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Literature DB >> 4942534

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

Abstract

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 gamma-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.

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Year: 1971 PMID： 4942534 PMCID： PMC1176919 DOI： 10.1042/bj1230163

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

24 in total

Review 1. Covalent labeling of active sites.

Authors: S J Singer
Journal: Adv Protein Chem Date: 1967

2. Kinetics of triose phosphate isomerase.

Authors: P M Burton; S G Waley
Journal: Biochim Biophys Acta Date: 1968-03-25

3. A convenient spectrophotometric procedure for the determination of amino-terminal tyrosine residues.

Authors: M Wilchek; T Spande; B Witkop
Journal: Biochemistry Date: 1968-05 Impact factor: 3.162

4. Studies on rabbit muscle enolase. Evicence for two identical polypeptide chains and two substrate binding sites in the active enzyme.

Authors: J M Cardenas; F Wold
Journal: Biochemistry Date: 1968-08 Impact factor: 3.162

5. Effect of alkylguanidines on the inactivation of trypsin by alkylation and phosphorylation.

Authors: T Inagami; H Hatano
Journal: J Biol Chem Date: 1969-03-10 Impact factor: 5.157

6. The identification of a glutamic acid residue as part of the active site of ribonuclease T-1.

Authors: K Takahashi; W H Stein; S Moore
Journal: J Biol Chem Date: 1967-10-25 Impact factor: 5.157

7. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.

Authors: R E Offord
Journal: Nature Date: 1966-08-06 Impact factor: 49.962

8. The active centre of triose phosphate isomerase.

Authors: P M Burton; S G Waley
Journal: Biochem J Date: 1966-09 Impact factor: 3.857

9. The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.

Authors: D R Trentham; C H McMurray; C I Pogson
Journal: Biochem J Date: 1969-08 Impact factor: 3.857

10. Phosphonomycin: structure and synthesis.

Authors: B G Christensen; W J Leanza; T R Beattie; A A Patchett; B H Arison; R E Ormond; F A Kuehl; G Albers-Schonberg; O Jardetzky
Journal: Science Date: 1969-10-03 Impact factor: 47.728

11 in total

1. The amino acid sequence of rabbit muscle triose phosphate isomerase.

Authors: P H Corran; S G Waley
Journal: Biochem J Date: 1975-02 Impact factor: 3.857

2. High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: the conformational flexibility of the catalytic glutamate in its closed, liganded active site.

Authors: Rajaram Venkatesan; Markus Alahuhta; Petri M Pihko; Rik K Wierenga
Journal: Protein Sci Date: 2011-07-07 Impact factor: 6.725

3. A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.

Authors: John P Richard
Journal: Biochemistry Date: 2012-03-20 Impact factor: 3.162

4. The tryptic peptides of rabbit muscle triose phosphate isomerase.

Authors: P H Corran; S G Waley
Journal: Biochem J Date: 1974-04 Impact factor: 3.857

5. Studies of triose phosphate isomerase by hydrogen exchange.

Authors: C A Browne; S G Waley
Journal: Biochem J Date: 1974-09 Impact factor: 3.857

6. The pK of the carboxyl group at the active centre of triose phosphate isomerase.

Authors: S G Waley
Journal: Biochem J Date: 1972-01 Impact factor: 3.857

7. Enzyme-substrate and enzyme-inhibitor complexes of triose phosphate isomerase studied by 31P nuclear magnetic resonance.

Authors: I D Campbell; R B Jones; P A Kiener; S G Waley
Journal: Biochem J Date: 1979-06-01 Impact factor: 3.857