Linked Life Data

9571033

Source:http://linkedlifedata.com/resource/pubmed/id/9571033

Statements in which the resource exists.
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pubmed-article:9571033pubmed:abstractTextThe binding site for the acceptor substrate poly(ADP-ribose) in the elongation reaction of the ADP-ribosyl transferase poly(ADP-ribose) polymerase (PARP) was detected by cocrystallizing the enzyme with an NAD+ analogue. The site was confirmed by mutagenesis studies. In conjunction with the binding site of the donor NAD+, the bound acceptor reveals the geometry of the elongation reaction. It shows in particular that the strictly conserved glutamate residue of all ADP-ribosylating enzymes (Glu988 of PARP) facilitates the reaction by polarizing both, donor and acceptor. Moreover, the binding properties of the acceptor site suggest a mechanism for the branching reaction, that also explains the dual specificity of this transferase for elongation and branching, which is unique among polymer-forming enzymes.lld:pubmed
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pubmed-article:9571033pubmed:authorpubmed-author:SchulzG EGElld:pubmed
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pubmed-article:9571033pubmed:copyrightInfoCopyright 1998 Academic Press Limited.lld:pubmed
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pubmed-article:9571033pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9571033pubmed:year1998lld:pubmed
pubmed-article:9571033pubmed:articleTitleThe mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis.lld:pubmed
pubmed-article:9571033pubmed:affiliationInstitut für Organische Chemie und Biochemie, Albertstr. 21, Freiburg im Breisgau, D-79104, Germany.lld:pubmed
pubmed-article:9571033pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9571033pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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