Linked Life Data

11106178

Source:http://linkedlifedata.com/resource/pubmed/id/11106178

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2001-2-20
pubmed:abstractText
The three-dimensional (3D) structure of Corynebacterium glutamicum diaminopimelate D-dehydrogenase in a ternary complex with NADPH and L-2-amino-6-methylene-pimelate has been solved and refined to a resolution of 2.1 A. L-2-Amino-6-methylene-pimelate was recently synthesized and shown to be a potent competitive inhibitor (5 microM) vs. meso-diaminopimelate of the Bacillus sphaericus dehydrogenase (Sutherland et al., 1999). Diaminopimelate dehydrogenase catalyzes the reversible NADP+ -dependent oxidation of the D-amino acid stereocenter of mesodiaminopimelate, and is the only enzyme known to catalyze the oxidative deamination of a D-amino acid. The enzyme is involved in the biosynthesis of meso-diaminopimelate and L-lysine from L-aspartate, a biosynthetic pathway of considerable interest because it is essential for growth of certain bacteria. The dehydrogenase is found in a limited number of species of bacteria, as opposed to the alternative succinylase and acetylase pathways that are widely distributed in bacteria and plants. The structure of the ternary complex reported here provides a structural rationale for the nature and potency of the inhibition exhibited by the unsaturated L-2-amino-6-methylene-pimelate against the dehydrogenase. In particular, we compare the present structure with other structures containing either bound substrate, meso-diaminopimelate, or a conformationally restricted isoxazoline inhibitor. We have identified a significant interaction between the alpha-L-amino group of the unsaturated inhibitor and the indole ring of Trp144 that may account for the tight binding of this inhibitor.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-10029526, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-1906065, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-3089835, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-3172202, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-3588313, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-8263917, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-8504824, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-8591046, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-8885833, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-8919551, http://linkedlifedata.com/resource/pubmed/commentcorrection/11106178-9521647
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2034-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate.
pubmed:affiliation
Instituto Strutturista Chimica - CNR, Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't