Literature DB >> 3036180

Carbamate kinase of Lactobacillus buchneri NCDO110. II. Kinetic studies and reaction mechanism.

M C Manca de Nadra, A A Pesce de Ruiz Holgado, G Oliver.   

Abstract

The participation of Mg2+ or Mn2+ nucleoside diphosphates in the reverse reaction catalyzed by purified carbamate kinase (ATP:carbamate phosphotransferase, EC 2.7.2.2) of Lactobacillus buchneri NCDO110 was studied. The results of initial velocity studies have indicated that Mn2+ ADP is as effective as a substrate as Mg2+ ADP is. Product inhibition studies have revealed that the enzyme has two distinct sites, one for nucleoside diphosphate and the other for carbamyl phosphate. The reaction of the enzyme with the substrates is of the random type.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3036180

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN: 0885-4513            Impact factor:   2.431


  1 in total

1.  Characterization of thermophilic archaeal isopentenyl phosphate kinases.

Authors:  Mo Chen; C Dale Poulter
Journal:  Biochemistry       Date:  2010-01-12       Impact factor: 3.162

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.