Home LiteratureArticle Details
PMID: 5969283 Published · ppublish English Journal Article

The active centre of triose phosphate isomerase.

The Biochemical journal ·Vol. 100 ·No. 3 ·1966-09-00 ·Pages 702-10

Burton PM, Waley SG

Abstract

The molecular weight and amino acid composition of triose phosphate isomerase have been determined. The molecular weight (43000) is lower and the molecular activity (500000) higher than those of most other glycolytic enzymes. Reaction with iodoacetate (studied with radioactive reagent) takes place in two phases: in the first phase, at pH6.3, cysteine and methionine groups react and enzymic activity is unimpaired; in the second phase, histidine reacts and enzymic activity is lost. Photo-oxidation leads to inactivation, with loss of cysteine, of histidine and of tryptophan, but little loss of tyrosine. The mechanism postulated for the action of the enzyme demands the intervention of a group functioning as a base, and the results obtained are consistent with histidine's being the basic group in the active centre.

MeSH Terms
Amino Acids/analysis Animals Carbon Isotopes Chromatography, Paper Electrophoresis Isomerases/analysis Molecular Weight Peptides/analysis Rabbits Sulfhydryl Compounds/analysis
Chemicals
Amino Acids Carbon Isotopes Peptides Sulfhydryl Compounds Isomerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Burton P M
Waley S G
References (26)
26 references, click to expand
  1. THE REACTIVITIES OF THE HISTIDINE RESIDUES AT THE ACTIVE SITE OF RIBONUCLEASE TOWARD HALO ACIDS OF DIFFERENT STRUCTURES.
    J Biol Chem. 1965 Jul;240:2921-34 PMID: 14342316
  2. Intramolecular hydrogen transfer in the phosphoglucose isomerase reaction.
    J Biol Chem. 1961 Dec;236:3086-92 PMID: 14493830
  3. [Simplification and improvement in the method for the quantitative determination of amino acids and peptides by means of ninhydrin-copper complexes].
    Biochem Z. 1955;326(6):433-5 PMID: 13239619
  4. [Quantitative determination of amino acid composition of protein hydrolysates by combined electrophoresis and chromatography].
    Hoppe Seylers Z Physiol Chem. 1955;299(5-6):258-76 PMID: 14391846
  5. Degradation, structure and some derivatives of cephalosporin N.
    Biochem J. 1954 Sep;58(1):103-11 PMID: 13198859
  6. The thiol groups of yeast alcohol dehydrogenase.
    Biochem J. 1964 Mar;90(3):532-9 PMID: 4284172
  7. The reaction of iodoacetate with methionine.
    J Biol Chem. 1959 Jul;234(7):1761-4 PMID: 13672959
  8. The action of trypsin on polylysine.
    Biochem J. 1953 Sep;55(2):328-37 PMID: 13093686
  9. Characterization of a human macroglobulin. II. Distribution of the disulfide bonds.
    J Biol Chem. 1965 Dec;240(12):4740-5 PMID: 5846989
  10. Tetrose diphosphate, a specific inhibitor of glyceraldehyde 3-phosphate dehydrogenase.
    J Biol Chem. 1959 Oct;234:2510-6 PMID: 14435686
  11. Starch gel electrophoresis in a discontinous system of buffers.
    Nature. 1957 Dec 28;180(4600):1477-9 PMID: 13493570
  12. The gel-filtration behaviour of proteins related to their molecular weights over a wide range.
    Biochem J. 1965 Sep;96(3):595-606 PMID: 5862401
  13. The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate.
    J Biol Chem. 1959 Jul;234(7):1754-60 PMID: 13672958
  14. PHOSPHOGLUCOSE ISOMERASE. II. INFLUENCE OF PH ON KINETIC PARAMETERS.
    Biochemistry. 1963 Jul-Aug;2:770-5 PMID: 14075112
  15. Acidic peptides of the lens.
    Biochem J. 1956 Dec;64(4):715-26 PMID: 13382824
  16. CARBOXYMETHYLATION OF SPERM WHALE METMYOGLOBIN.
    J Biol Chem. 1963 Oct;238:3307-14 PMID: 14085377
  17. The determination of triose phosphate isomerase.
    Arch Biochem. 1950 Jun;27(1):223-33 PMID: 15419792
  18. Carboxymethylamino acids and peptides.
    J Biol Chem. 1956 Jul;221(1):113-31 PMID: 13345804
  19. Tissue sulfhydryl groups.
    Arch Biochem Biophys. 1959 May;82(1):70-7 PMID: 13650640
  20. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults.
    Biochem J. 1955 Dec;61(4):629-41 PMID: 13276348
  21. A method for characterizing the type and numbers of groups involved in enzyme action.
    J Biol Chem. 1961 Jul;236:1973-9 PMID: 13739952
  22. The mechanism of the triosephosphate isomerase reaction.
    J Biol Chem. 1959 May;234(5):1007-10 PMID: 13654309
  23. Trypsin-catalysed transpeptidations.
    Biochem J. 1954 Aug;57(4):529-38 PMID: 13198796
  24. Alkylation and identification of the histidine residues at the active site of ribonuclease.
    J Biol Chem. 1963 Jul;238:2413-9 PMID: 14023809
  25. Mechanism of C-H bond cleavage in aldolase and isomerase reactions.
    Brookhaven Symp Biol. 1962 Dec;15:293-309 PMID: 13974790
  26. A new technique for the analysis of histidine, tyrosine, methionine and arginine in protein hydrolysates.
    Arch Biochem Biophys. 1956 Nov;65(1):296-301 PMID: 13373426
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1000702
Published
1966-09-00
Pages
702-10
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1265204
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1000702 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