Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase

J Mikkelsen; P Højrup; H F Hansen; J K Hansen; J Knudsen

doi:10.1042/bj2270981

Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase

J Mikkelsen, P Højrup, H F Hansen, J K Hansen, J Knudsen

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

Competitive binding experiments with malonyl-CoA and [1-14C]acetyl-CoA, [1-14C]butyryl-CoA or [1-14C]decanoyl-CoA indicate that all these substrates are transferred to lactating-goat mammary-gland fatty acid synthetase by the same transferase. Isolation and determination of the amino acid sequence of [1-14C]decanoyl-labelled CNBr-cleavage peptide from the decanoyltransferase site showed that this transferase is identical with the acetyl/malonyltransferase.

Original language	English
Journal	Biochemical Journal
Volume	227
Issue number	3
Pages (from-to)	981-5
Number of pages	5
ISSN	0264-6021
DOIs	https://doi.org/10.1042/bj2270981
Publication status	Published - 1. May 1985

Keywords

Acetyl Coenzyme A/metabolism
Acyl Coenzyme A/metabolism
Acyltransferases/metabolism
Amino Acid Sequence
Animals
Binding Sites
Fatty Acid Synthases/metabolism
Female
Formates/metabolism
Goats
Lactation
Malonyl Coenzyme A/metabolism
Mammary Glands, Animal/enzymology
Pregnancy

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10.1042/bj2270981

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title = "Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase",

abstract = "Competitive binding experiments with malonyl-CoA and [1-14C]acetyl-CoA, [1-14C]butyryl-CoA or [1-14C]decanoyl-CoA indicate that all these substrates are transferred to lactating-goat mammary-gland fatty acid synthetase by the same transferase. Isolation and determination of the amino acid sequence of [1-14C]decanoyl-labelled CNBr-cleavage peptide from the decanoyltransferase site showed that this transferase is identical with the acetyl/malonyltransferase.",

keywords = "Acetyl Coenzyme A/metabolism, Acyl Coenzyme A/metabolism, Acyltransferases/metabolism, Amino Acid Sequence, Animals, Binding Sites, Fatty Acid Synthases/metabolism, Female, Formates/metabolism, Goats, Lactation, Malonyl Coenzyme A/metabolism, Mammary Glands, Animal/enzymology, Pregnancy",

author = "J Mikkelsen and P H{\o}jrup and Hansen, {H F} and Hansen, {J K} and J Knudsen",

year = "1985",

month = may,

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doi = "10.1042/bj2270981",

language = "English",

volume = "227",

pages = "981--5",

journal = "Biochemical Journal",

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TY - JOUR

T1 - Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase

AU - Mikkelsen, J

AU - Højrup, P

AU - Hansen, H F

AU - Hansen, J K

AU - Knudsen, J

PY - 1985/5/1

Y1 - 1985/5/1

N2 - Competitive binding experiments with malonyl-CoA and [1-14C]acetyl-CoA, [1-14C]butyryl-CoA or [1-14C]decanoyl-CoA indicate that all these substrates are transferred to lactating-goat mammary-gland fatty acid synthetase by the same transferase. Isolation and determination of the amino acid sequence of [1-14C]decanoyl-labelled CNBr-cleavage peptide from the decanoyltransferase site showed that this transferase is identical with the acetyl/malonyltransferase.

AB - Competitive binding experiments with malonyl-CoA and [1-14C]acetyl-CoA, [1-14C]butyryl-CoA or [1-14C]decanoyl-CoA indicate that all these substrates are transferred to lactating-goat mammary-gland fatty acid synthetase by the same transferase. Isolation and determination of the amino acid sequence of [1-14C]decanoyl-labelled CNBr-cleavage peptide from the decanoyltransferase site showed that this transferase is identical with the acetyl/malonyltransferase.

KW - Acetyl Coenzyme A/metabolism

KW - Acyl Coenzyme A/metabolism

KW - Acyltransferases/metabolism

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Fatty Acid Synthases/metabolism

KW - Female

KW - Formates/metabolism

KW - Goats

KW - Lactation

KW - Malonyl Coenzyme A/metabolism

KW - Mammary Glands, Animal/enzymology

KW - Pregnancy

U2 - 10.1042/bj2270981

DO - 10.1042/bj2270981

M3 - Journal article

C2 - 4004809

SN - 0264-6021

VL - 227

SP - 981

EP - 985

JO - Biochemical Journal

JF - Biochemical Journal

IS - 3

ER -

Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase

Abstract

Keywords

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