Literature DB >> 4359463

Aspartate transcarbamylase from Streptococcus faecalis. Steady-state kinetic analysis.

T Y Chang, M E Jones.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1974        PMID： 4359463     DOI： 10.1021/bi00701a002

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


× No keyword cloud information.
  2 in total

1.  Wheat-germ aspartate transcarbamoylase. Steady-state kinetics and stereochemistry of the binding site for L-aspartate.

Authors:  J E Grayson; R J Yon; P J Butterworth
Journal:  Biochem J       Date:  1979-11-01       Impact factor: 3.857

2.  Structural and regulatory mutations allowing utilization of citrulline or carbamoylaspartate as a source of carbamoylphosphate in Escherichia coli K-12.

Authors:  C Legrain; V Stalon; N Glansdorff; D Gigot; A Piéard; M Crabeel
Journal:  J Bacteriol       Date:  1976-10       Impact factor: 3.490
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.