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

M. Fisher; J.T.M. Kroon; W. Martindale; A.R. Stuitje; A.R. Slabas; J.B. Rafferty

doi:10.1016/S0969-2126(00)00115-5

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

M. Fisher, J.T.M. Kroon, W. Martindale, A.R. Stuitje, A.R. Slabas, J.B. Rafferty

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 Å resolution in a binary complex with an NADP

Original language	English
Pages (from-to)	339-347
Number of pages	9
Journal	Structure
Volume	8
DOIs	https://doi.org/10.1016/S0969-2126(00)00115-5
Publication status	Published - 2000

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/S0969-2126(00)00115-5

Persistent URL (handle)

Persistent link

Cite this

@article{44a803c03a964443aac97e589e1186a9,

title = "The X-ray structure of Brassica napus {\ss}-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.",

abstract = "Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 {\AA} resolution in a binary complex with an NADP",

author = "M. Fisher and J.T.M. Kroon and W. Martindale and A.R. Stuitje and A.R. Slabas and J.B. Rafferty",

year = "2000",

doi = "10.1016/S0969-2126(00)00115-5",

language = "English",

volume = "8",

pages = "339--347",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

}

TY - JOUR

T1 - The X-ray structure of Brassica napus ß-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.

AU - Fisher, M.

AU - Kroon, J.T.M.

AU - Martindale, W.

AU - Stuitje, A.R.

AU - Slabas, A.R.

AU - Rafferty, J.B.

PY - 2000

Y1 - 2000

N2 - Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 Å resolution in a binary complex with an NADP

AB - Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 Å resolution in a binary complex with an NADP

U2 - 10.1016/S0969-2126(00)00115-5

DO - 10.1016/S0969-2126(00)00115-5

M3 - Article

SN - 0969-2126

VL - 8

SP - 339

EP - 347

JO - Structure

JF - Structure

ER -

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

Abstract

UN SDGs

Access to Document

Persistent URL (handle)

Fingerprint

Cite this