Evolution of NAD biosynthetic enzymes

Charles Brenner

doi:10.1016/j.str.2005.08.004

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Journal article

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Evolution of NAD biosynthetic enzymes

Charles Brenner

Structure (London, England : 1993), Vol.13(9), pp.1239-1240

09/2005

DOI: 10.1016/j.str.2005.08.004

PMID: 16154080

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Abstract

Two research groups have solved crystal structures of nicotinic acid phosphoribosyltransferase (PRTase) and made the argument that PRTases in three distinct pathways of nicotinamide adenine dinucleotide (NAD) biosynthesis evolved from a common ancestor (Shin et al., 2005 and Chappie et al., 2005).

Pentosyltransferases - genetics

Protein Conformation

Pentosyltransferases - chemistry

NAD - biosynthesis

Evolution, Molecular

Details

Title: Subtitle: Evolution of NAD biosynthetic enzymes
Creators: Charles Brenner - Department of Genetics, Dartmouth Medical School,Lebanon, NH 03756, USA
Resource Type: Journal article
Publication Details: Structure (London, England : 1993), Vol.13(9), pp.1239-1240
Publisher: United States
DOI: 10.1016/j.str.2005.08.004
PMID: 16154080
ISSN: 0969-2126
eISSN: 1878-4186
Language: English
Date published: 09/2005
Academic Unit: Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9983788431402771

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