A snapshot of carnitine acetyltransferase

Rona Ruth Ramsay; James Henderson Naismith

doi:10.1016/S0968-0004(03)00137-3

A snapshot of carnitine acetyltransferase

Rona Ruth Ramsay, James Henderson Naismith

Research output: Contribution to journal › Article › peer-review

Abstract

Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.

Original language	English
Pages (from-to)	343-346
Number of pages	4
Journal	Trends in Biochemical Sciences
Volume	28
Issue number	7
DOIs	https://doi.org/10.1016/S0968-0004(03)00137-3
Publication status	Published - Jul 2003

Keywords

TRANSITION-STATE STABILIZATION
CATALYTIC MECHANISM
CRYSTAL-STRUCTURE
ACYLTRANSFERASES
PALMITOYLTRANSFERASE
ENZYMOLOGY
TRANSPORT
BINDING
ACID

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title = "A snapshot of carnitine acetyltransferase",

abstract = "Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.",

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AU - Ramsay, Rona Ruth

AU - Naismith, James Henderson

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N2 - Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.

AB - Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.

KW - TRANSITION-STATE STABILIZATION

KW - CATALYTIC MECHANISM

KW - CRYSTAL-STRUCTURE

KW - ACYLTRANSFERASES

KW - PALMITOYLTRANSFERASE

KW - ENZYMOLOGY

KW - TRANSPORT

KW - BINDING

KW - ACID

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JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 7

ER -

A snapshot of carnitine acetyltransferase

Abstract

Keywords

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