Transacylase activity of lactating bovine mammary fatty acid synthase

Gregory J. Anderson; Soma Kumar

doi:10.1016/0014-5793(87)80839-6

Transacylase activity of lactating bovine mammary fatty acid synthase

Gregory J. Anderson, Soma Kumar

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

4 Scopus citations

Abstract

An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [³H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.

Original language	English (US)
Pages (from-to)	323-326
Number of pages	4
Journal	FEBS Letters
Volume	220
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(87)80839-6
State	Published - Aug 17 1987
Externally published	Yes

Keywords

Acyl exchange
Fatty acid synthase
Substrate specificity
Transacylase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(87)80839-6

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title = "Transacylase activity of lactating bovine mammary fatty acid synthase",

abstract = "An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [3H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.",

keywords = "Acyl exchange, Fatty acid synthase, Substrate specificity, Transacylase",

author = "Anderson, {Gregory J.} and Soma Kumar",

note = "Funding Information: This work was supported in part by National Institutes of Health research grant AM, 16086,",

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T1 - Transacylase activity of lactating bovine mammary fatty acid synthase

AU - Anderson, Gregory J.

AU - Kumar, Soma

N1 - Funding Information: This work was supported in part by National Institutes of Health research grant AM, 16086,

PY - 1987/8/17

Y1 - 1987/8/17

N2 - An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [3H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.

AB - An assay for the transacylation reaction catalyzed by fatty acid synthase was developed which does not require model substrates or labelled acyl-derivatives of CoA. It involves the transfer of the acyl group from unlabelled CoA to [3H]CoA. This assay shows the occurrence of transacylation at a relatively high rate with a variety of substrates that the enzyme is able to utilize. The activity is unaffected by dissociation of the enzyme or modification by iodoacetamide or 2-chloroacetyl-CoA.

KW - Acyl exchange

KW - Fatty acid synthase

KW - Substrate specificity

KW - Transacylase

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JF - FEBS Letters

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ER -

Transacylase activity of lactating bovine mammary fatty acid synthase

Abstract

Keywords

ASJC Scopus subject areas

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