2000
DOI: 10.1016/s0969-2126(00)00115-5
|View full text |Cite
|
Sign up to set email alerts
|

The X-ray structure of Brassica napus β-keto acyl carrier protein reductase and its implications for substrate binding and catalysis

Abstract: A catalytic mechanism can be proposed involving the conserved triad. Helix alpha6 must shift its position to permit substrate binding to BKR and might act as a flexible lid on the active site. The similarities in fold, mechanism and substrate binding between BKR, which catalyzes a carbon-oxygen double-bond reduction, and ENR, the carbon-carbon double-bond oxidoreductase in FAS, suggest a close evolutionary link during the development of the fatty acid biosynthetic pathway.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

6
88
1
1

Year Published

2001
2001
2015
2015

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 91 publications
(96 citation statements)
references
References 39 publications
6
88
1
1
Order By: Relevance
“…The cofactor requirement for the mammalian microsomal KCR protein has not been settled yet [29,30]. The plant 3-ketoacy-[acyl carrier protein] reductase involved in plastid fatty acid synthesis was NADPH-dependent [31]. NADPH binding was found to induce a conformational change that put three conserved amino acid residues into the active site to facilitate catalytic function [32].…”
Section: Discussionmentioning
confidence: 99%
“…The cofactor requirement for the mammalian microsomal KCR protein has not been settled yet [29,30]. The plant 3-ketoacy-[acyl carrier protein] reductase involved in plastid fatty acid synthesis was NADPH-dependent [31]. NADPH binding was found to induce a conformational change that put three conserved amino acid residues into the active site to facilitate catalytic function [32].…”
Section: Discussionmentioning
confidence: 99%
“…Nevertheless, the deposited structure of HsHSD17B8 (PDB id: 2PD6) shows that this protein can form homotetramers in the absence of CBR4. The observed heterotetrameric arrangement of HsKAR is similar to the homotetrameric orthologues of HsKAR, for example, from B. napus and E. coli 13,14 , and the two subunits interact in an optimal way, providing higher stability to the heterotetramer than to the respective homotetramers.…”
Section: Discussionmentioning
confidence: 57%
“…2c), demonstrating the cofactor preference of the two subunits. The conformation of NAD þ and NADP þ in the respective binding sites are similar to that of NADP þ in Brassica napus (B. napus) and E. coli fabG 13,15 . Both NAD þ and NADP þ are stabilized by many conserved hydrogen bonding interactions in their respective binding sites ( Fig.…”
Section: Resultsmentioning
confidence: 86%
See 2 more Smart Citations