Home LiteratureArticle Details
PMID: 4377107 Published · ppublish English Journal Article

Kinetic studies of bovine liver carbamoyl phosphate synthetase.

The Biochemical journal ·Vol. 141 ·No. 3 ·1974-09-00 ·Pages 807-16

Elliott KR, Tipton KF

Abstract

A through study of initial-rate data has been made on carbamoyl phosphate synthetase from bovine liver. On the basis of the results the order of substrate binding to the enzyme is ATPMg followed by HCO(3) (-), ATPMg and NH(4) (+). A model for the enzymic mechanism is proposed, and the rate equations describing it are presented. Details of the derivation of the initial-rate equation for the kinetic mechanism proposed have been deposited as Supplementary Publication SUP 50032 (6 pages) at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7QB, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

MeSH Terms
Adenosine Triphosphate Animals Bicarbonates Cattle Glutamates Kinetics Liver/enzymology Magnesium Models, Chemical Phosphotransferases/metabolism Quaternary Ammonium Compounds
Chemicals
Bicarbonates Glutamates Quaternary Ammonium Compounds Adenosine Triphosphate Phosphotransferases Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Elliott K R
Tipton K F
References (13)
13 references, click to expand
  1. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state.
    J Biol Chem. 1968 Feb 25;243(4):820-5 PMID: 5638598
  2. Kinetic studies on rat liver carbamyl phosphate synthetase.
    J Biol Chem. 1968 Aug 25;243(16):4279-85 PMID: 5679964
  3. Structure and function of carbamoylphosphate synthase. I. Transitions between two catalytically inactive forms and the active form.
    Eur J Biochem. 1968 Dec;7(1):119-27 PMID: 5751125
  4. Structure and function of carbamoylphosphate synthetase. On the mechanism of bicarbonate activation.
    Eur J Biochem. 1969 Mar;8(2):207-14 PMID: 5781273
  5. Purification and characterisation of carbamoyl phosphate synthetase from beef liver.
    FEBS Lett. 1973 Nov 15;37(1):79-81 PMID: 4753763
  6. A kinetic analysis of enzyme systems involving four substrates.
    Biochem J. 1974 Sep;141(3):789-805 PMID: 4463962
  7. STUDIES ON THE MECHANISM OF ACTION OF ACETYLGLUTAMATE AS AN ACTIVATOR OF CARBAMYL PHOSPHATE SYNTHETASE.
    J Biol Chem. 1964 Jun;239:1935-41 PMID: 14213380
  8. Studies on the biosynthesis of carbamyl phosphate.
    J Biol Chem. 1957 Dec;229(2):1019-25 PMID: 13502361
  9. Isolation and characterization of a naturally occurring cofactor of carbamyl phosphate biosynthesis.
    J Biol Chem. 1958 Feb;230(2):1013-21 PMID: 13525417
  10. Purification of carbamyl phosphate synthetase from frog liver.
    J Biol Chem. 1958 Jul;233(1):102-5 PMID: 13563449
  11. Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions.
    Biochem J. 1959 Feb;71(2):388-95 PMID: 13628582
  12. A KINETIC STUDY OF CARBAMYL PHOSPHATE SYNTHETASE.
    J Biol Chem. 1964 Jun;239:1925-34 PMID: 14213379
  13. Product inhibition studies on bovine liver carbamoyl phosphate synthetase.
    Biochem J. 1974 Sep;141(3):817-24 PMID: 4377108
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1974-09-00
Pages
807-16
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1168186
Subset
IM
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]