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Article

Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases.

The Journal of biological chemistry - 11 Jun 1999

Konczalik P, Moss J

Abstract excerpt

NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyze opposing arms of a putative ADP-ribosylation cycle. ADP-ribosylarginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarity in deduced amino acid sequence. We postulated that amino acids in these consensus regions could be critical for hydrolase function. To test this hypothesis, hydrolase,...

Topics

Adenosine Diphosphate Ribose
Amino Acid Sequence
Animals
Aspartic Acid
Brain
Cloning, Molecular
Conserved Sequence
Escherichia coli
Glycoside Hydrolases
Mutation
N-Glycosyl Hydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Processing, Post-Translational

Rats

Recombinant Fusion Proteins

Rhodospirillum rubrum

Species Specificity

Source

Identifiers

PMID: 10358013
DOI: 10.1074/jbc.274.24.16736

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