Literature DB >> 3518720

The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherichia coli.

K W Volź, K L Krause, W N Lipscomb.   

Abstract

A more precise description of the binding of N-(phosphonacetyl)-L- aspartate to the catalytic chains of aspartate carbamoyltransferase clarifies aspects of the specificity of this enzyme toward its substrates, carbamoylphosphate and L-aspartate, and suggests a catalytic role for His-134.

Entities:  

Mesh：

Substances：

Year:  1986        PMID： 3518720     DOI： 10.1016/0006-291x(86)90514-0

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

1.  Origin, structure, and regulation of argK, encoding the phaseolotoxin-resistant ornithine carbamoyltransferase in Pseudomonas syringae pv. phaseolicola, and functional expression of argK in transgenic tobacco.

Authors:  E Hatziloukas; N J Panopoulos
Journal:  J Bacteriol       Date:  1992-09       Impact factor: 3.490

2.  Molecular evolution of enzyme structure: construction of a hybrid hamster/Escherichia coli aspartate transcarbamoylase.

Authors:  J G Major; M E Wales; J E Houghton; J A Maley; J N Davidson; J R Wild
Journal:  J Mol Evol       Date:  1989-05       Impact factor: 2.395

3.  Active-site-directed inactivation of wheat-germ aspartate transcarbamoylase by pyridoxal 5'-phosphate.

Authors:  S C Cole; R J Yon
Journal:  Biochem J       Date:  1987-12-01       Impact factor: 3.857

4.  Patient selection may affect gene therapy success. Dominant negative effects observed for ornithine transcarbamylase in mouse and human hepatocytes.

Authors:  M A Morsy; J Z Zhao; T T Ngo; A W Warman; W E O'Brien; F L Graham; C T Caskey
Journal:  J Clin Invest       Date:  1996-02-01       Impact factor: 14.808
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.