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Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli.

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Garwin, J.L., Klages, A.L., Cronan, J.E.·1980·Journal of Biological Chemistry

Abstract

Beta-Ketoacyl-acyl carrier protein synthases I and II of Escherichia coli were purified and characterized. Synthase I was shown to have a molecular weight of 80,000 +/- 5,000 and to be composed of two similarly sized subunits. Synthase II had a molecular weight of 85,000 +/- 5,000 and also was apparently homodimeric. Gel electrophoresis of partial proteolytic digests demonstrated that synthases I and II share few if any common peptides. Synthases I and II also were shown to be unrelated by immunological criteria. An improved assay for beta-ketoacyl-acyl carrier protein synthase activity gave kinetic parameters for synthases I and II at both 27 degrees C and 37 degrees C using five long chain acyl-acyl carrier protein substrates. The properties of synthase II are consistent with the proposed role of this enzyme in the modulation of fatty acid synthesis by temperature. fabF mutants of E. coli lack synthase II. The fabF locus was mapped at min 24.5 of the E. coli genetic map and the clockwise map order was found to be pyrC, fabD, fabF, purB.

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Metadata

Authors
Garwin, J. L., Klages, A. L., & Cronan, J. E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1980-12
Volume
255
Issue
24
Pages
11949-11956
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1699689362
Cited by
207
References
0
FWCI
3.56
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. https://app.cochat.ai/papers/10.1016/s0021-9258(19)70226-9
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Garwin, J. L., Klages, A. L., & Cronan, J. E. (1980). Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)70226-9

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