Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli.
AUTOR(ES)
Konigsberg, W H
RESUMO
We propose a primary structure for the catalytic subunit of aspartate transcarbamoylase (aspartate carbamoyltransferase; carbamoylphosphate: L-aspartate carbamoyltransferase, EC 2.1.3.2) from Escherichia coli based on amino acid sequences of fragments obtained by cyanogen bromide cleavage, by tryptic digestion of the succinylated polypeptide, and by chymotryptic and proteinase C digestion of the intact catalytic chain. The protein contains 310 amino acids and has a calculated molecular weight of 33,944. The negatively and positively charged residues are distributed uniformly, and there is no indication of charge clustering in the linear sequence.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=393846Documentos Relacionados
- Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli.
- Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.
- 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
- Allosteric Regulation of Catalytic Activity: Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase
- The amino acid sequence of beta-galactosidase of Escherichia coli.