Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model (Q28141751)

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scientific article (publication date: 23 April 1999)

Language	Label	Description	Also known as
English	Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model	scientific article (publication date: 23 April 1999)

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scholarly article

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Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model (English)

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author name string

A Witkowski

1

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A K Joshi

2

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V S Rangan

3

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A M Falick

4

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H E Witkowska

5

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S Smith

6

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language of work or name

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publication date

23 April 1999

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Journal of Biological Chemistry

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274

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17

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11557-63

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Fatty acid synthase, a proficient multifunctional enzyme

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https://api.crossref.org/works/10.1074%2FJBC.274.17.11557

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Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast

1 reference

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Mechanism of dissociation of pigeon liver fatty acid synthetase complex into half-molecular weight subunits and their reassociation to enzymatically active complex

1 reference

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Fatty acid synthesis and its regulation

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Rat mammary gland fatty acid synthase: localization of the constituent domains and two functional polyadenylation/termination signals in the cDNA

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Molecular cloning and sequencing of cDNAs encoding the entire rat fatty acid synthase

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Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA.

1 reference

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Characterization of fatty acid synthase monomers restrained from reassociating by immobilization to a solid support

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Fatty acid synthase: in vitro complementation of inactive mutants

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Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro

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The Malonyl/Acetyltransferase and β-Ketoacyl Synthase Domains of the Animal Fatty Acid Synthase Can Cooperate with the Acyl Carrier Protein Domain of Either Subunit

1 reference

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21 January 2018

Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunits

1 reference

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Construction of a cDNA encoding the multifunctional animal fatty acid synthase and expression in Spodoptera frugiperda cells using baculoviral vectors

1 reference

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Differential Affinity Labeling of the Two Subunits of the Homodimeric Animal Fatty Acid Synthase Allows Isolation of Heterodimers Consisting of Subunits That Have Been Independently Modified

1 reference

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8 Fatty acid synthase from lactating rat mammary gland

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Characterization of the Interthiol Acyltransferase Reaction Catalyzed by the β-Ketoacyl Synthase Domain of the Animal Fatty Acid Synthase

1 reference

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21 January 2018

Sample immobilization protocols for matrix-assisted laser-desorption mass spectrometry

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Structural organization of the multifunctional animal fatty-acid synthase

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Mammalian fatty acid synthetase is a structurally and functionally symmetrical dimer

1 reference

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21 January 2018

Identifiers

10.1074/JBC.274.17.11557

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