Home LiteratureArticle Details
PMID: 4942534 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 123 ·No. 2 ·1971-06-00 ·Pages 163-70

Miller JC, Waley SG

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.

MeSH Terms
1-Propanol Amino Acid Sequence Animals Binding Sites Electrophoresis Esters Ethers, Cyclic Glutamates Isomerases/analysis Models, Chemical Pepsin A Peptides/analysis Phosphorus Isotopes Rabbits
Chemicals
Esters Ethers, Cyclic Glutamates Peptides Phosphorus Isotopes 1-Propanol Pepsin A Isomerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Miller J C
Waley S G
References (24)
24 references, click to expand
  1. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.
    Nature. 1966 Aug 6;211(5049):591-3 PMID: 5968723
  2. The active centre of triose phosphate isomerase.
    Biochem J. 1966 Sep;100(3):702-10 PMID: 5969283
  3. The identification of a glutamic acid residue as part of the active site of ribonuclease T-1.
    J Biol Chem. 1967 Oct 25;242(20):4682-90 PMID: 6061414
  4. Kinetics of triose phosphate isomerase.
    Biochim Biophys Acta. 1968 Mar 25;151(3):714-5 PMID: 5646052
  5. A convenient spectrophotometric procedure for the determination of amino-terminal tyrosine residues.
    Biochemistry. 1968 May;7(5):1787-91 PMID: 5650381
  6. Studies on rabbit muscle enolase. Evicence for two identical polypeptide chains and two substrate binding sites in the active enzyme.
    Biochemistry. 1968 Aug;7(8):2736-41 PMID: 5666748
  7. Covalent labeling of active sites.
    Adv Protein Chem. 1967;22:1-54 PMID: 4883055
  8. Effect of alkylguanidines on the inactivation of trypsin by alkylation and phosphorylation.
    J Biol Chem. 1969 Mar 10;244(5):1176-82 PMID: 5812958
  9. The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.
    Biochem J. 1969 Aug;114(1):19-24 PMID: 4309306
  10. Phosphonomycin: structure and synthesis.
    Science. 1969 Oct 3;166(3901):123-5 PMID: 5821213
  11. Isolation and sequence of peptides at the active center of bovine carboxypeptidase B.
    J Biol Chem. 1969 Oct 10;244(19):5246-53 PMID: 5344132
  12. Inactivation and labeling of triose phosphate isomerase and enolase by glycidol phosphate.
    J Biol Chem. 1969 Dec 10;244(23):6548-50 PMID: 5389737
  13. Isolation and characterization of an active-site peptide from triose phosphate isomerase.
    J Am Chem Soc. 1970 Apr 8;92(7):2170-2 PMID: 5461608
  14. Partial sequence of an active-site peptide from triose phosphate isomerase.
    Biochem Biophys Res Commun. 1970 May 11;39(3):384-8 PMID: 5421940
  15. Uniquely labelled active site sequence in chicken muscle triose phosphate isomerase.
    Nature. 1970 Jul 11;227(5254):180-1 PMID: 5428407
  16. Identification of site in triose phosphate isomerase labelled by glycidol phosphate.
    Nature. 1970 Jul 11;227(5254):181 PMID: 5428408
  17. The isolation and crystallization of yeast and rabbit liver triose phosphate isomerase and a comparative characterization with the rabbit muscle enzyme.
    Eur J Biochem. 1970 Jun;14(2):289-300 PMID: 5506172
  18. Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase.
    Biochem J. 1971 Apr;122(2):209-18 PMID: 5165707
  19. Binding of substrate and transition state analog to trisephosphate isomerase.
    Biochemistry. 1970 Aug 18;9(17):3404-7 PMID: 5535476
  20. Colour reactions on paper chromatograms by a dipping technique.
    Nature. 1953 Jan 3;171(4340):43-4 PMID: 13025474
  21. [Amino acid determination on paper chromatograms].
    Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219-20 PMID: 13513014
  22. Thermodynamic quantities for the dissociation equilibria of biologically important compounds. 7. The second acid dissociation of glycerol 1-phosphates.
    Biochem J. 1958 Jun;69(2):218-23 PMID: 13546169
  23. Mechanism of C-H bond cleavage in aldolase and isomerase reactions.
    Brookhaven Symp Biol. 1962 Dec;15:293-309 PMID: 13974790
  24. THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551.
    Biochem J. 1963 Nov;89:349-78 PMID: 14084622
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1230163
Published
1971-06-00
Pages
163-70
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1176919
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1230163 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2