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PMID: 7898462 Published · ppublish English Journal Article

Common structure of the catalytic sites of mammalian and bacterial toxin ADP-ribosyltransferases.

Molecular and cellular biochemistry ·Vol. 138 ·No. 1-2 ·1994-09-00 ·Pages 177-81

Okazaki IJ, Moss J

Abstract

The amino acid sequences of several bacterial toxin ADP-ribosyltransferases, rabbit skeletal muscle transferases, and RT6.2, a rat T-cell NAD glycohydrolase, contain three separate regions of similarity, which can be aligned. Region I contains a critical histidine or arginine residue, region II, a group of closely spaced aromatic amino acids, and region III, an active-site glutamate which is at times seen as part of an acidic amino acid-rich sequence. In some of the bacterial ADP-ribosyltransferases, the nicotinamide moiety of NAD has been photo-crosslinked to this glutamate, consistent with its position in the active site. The similarities within these three regions, despite an absence of overall sequence similarity among the several transferases, are consistent with a common structure involved in NAD binding and ADP-ribose transfer.

MeSH Terms
Amino Acid Sequence Animals Bacterial Toxins/chemistry Catalysis Humans Molecular Sequence Data Poly(ADP-ribose) Polymerases/chemistry Rabbits Rats Sequence Homology, Amino Acid
Chemicals
Bacterial Toxins Poly(ADP-ribose) Polymerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Okazaki I J
Laboratory of Cellular Metabolism, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Moss J
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
DOI
10.1007/BF00928460
Published
1994-09-00
Pages
177-81
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00928460 View journal details
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