Regulation of fatty acid synthetase activity. The 4'-phosphopantetheine hydrolase of rat liver.

Sobhy, C.M.

doi:10.1016/s0021-9258(19)86929-6

Cited by 9 publications

(3 citation statements)

References 25 publications

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“…286 Later, a puried enzyme preparation was unambiguously shown to hydrolyze radioactive-pantetheine from labeled rat type I FAS (holo-FAS). 287 This was also the rst proof that the large type I FAS only carries one ACP, since the molar ratio of pantetheine released from the protein was 1 : 1. The puried enzyme preparation was not able to cleave the PPant arm from CoA or from pigeon liver holo-FAS, and the expression of the enzyme seems to vary with nutrition: the enzymatic activity was high in 3-day fasted rats, whereas no hydrolase activity was detected in 2-day fasted or normally fed rats.…”

Section: Regulation By 4 0 -Phosphopantetheinylationmentioning

confidence: 72%

“…The puried enzyme preparation was not able to cleave the PPant arm from CoA or from pigeon liver holo-FAS, and the expression of the enzyme seems to vary with nutrition: the enzymatic activity was high in 3-day fasted rats, whereas no hydrolase activity was detected in 2-day fasted or normally fed rats. 287 E. coli AcpH was recently expressed and puried. Further, AcpH activity must somehow be regulated in vivo, since based on the cellular levels of AcpH and its activity, it would transform all cellular holo-ACP into apo-ACP within one minute.…”

Section: Regulation By 4 0 -Phosphopantetheinylationmentioning

confidence: 99%

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The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

et al. 2014

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Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et al. in 1996 that PPTases garnered wide-spread attention being classified as a distinct enzyme superfamily. In the past two decades an increasing number of papers has been published on PPTases ranging from identification, characterization, structure determination, mutagenesis, inhibition, and engineering in synthetic biology. In this review, we comprehensively discuss all current knowledge on this class of enzymes that post-translationally install a 4′-phosphopantetheine arm on various carrier proteins.

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Section: Regulation By 4 0 -Phosphopantetheinylationmentioning

confidence: 72%

Section: Regulation By 4 0 -Phosphopantetheinylationmentioning

confidence: 99%

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

et al. 2014

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“…This is puzzling, as AcpH activity has been reported in a number of other organisms, including rat and pigeon. 206,207 Also, the best substrates for AcpH were found to be ACPs which are also substrates for the primary PPTase AcpS, 205 making it unlikely this particular enzyme would be useful in the study of NRPS enzymes. Still, the application of AcpH for the production of apo-ACPs from FAS and PKS systems represents an intriguing avenue for future use in combination with proteomic CP labeling methods.…”

Section: In Vitro Labeling Of Carrier Protein Domainsmentioning

confidence: 99%

The chemical biology of modular biosynthetic enzymes

2009

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Fatty acid synthase (FAS), polyketide synthase (PKS), and nonribosomal peptide synthetase (NRPS) modular biosynthetic enzymes are responsible for the production of a multitude of structurally diverse and biologically important small molecule natural products. Traditional biochemical and genetic studies of these enzymes have contributed substantially to the understanding of their underlying biosynthetic mechanisms. More recently these investigations have been aided by the skillful application of a combination of chemical and biological techniques to aid in overcoming the unique challenges associated with the enzymology of these large multifunctional enzymes. This critical review provides a historical context and details studies (through July 2008) which aim to identify and characterize these enzymes using synthetically and/or chemoenzymatically generated small molecule probes (233 references).

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Reaction of chloroacetyl‐CoA with rabbit fatty acid synthase

McCarthy

Hardie

1982

FEBS Letters

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The substrate analogue chloroacetyl-CoA inhibits fatty acid synthase by reacting with the 'central' or pantetheine thiol and not the 'peripheral' or fi-ketoacylsynthase thiol as previously reported. This was demonstrated by the isolation of [ 14C]carboxymethylcysteamine after acid hydrolysis of enzyme labelled with chloro(14C]acetyl-CoA, and by the demonstration that more than one of the partial reactions is inhibited. This reagent now represents a simple and convenient tool both for quantification of the pantetheine thiol and for labelling this site for peptide mapping and isolation.Fatty acid synthase Pantetheine Active-site label&g

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Regulation of fatty acid synthetase activity. The 4'-phosphopantetheine hydrolase of rat liver.

Cited by 9 publications

References 25 publications

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

The chemical biology of modular biosynthetic enzymes

Reaction of chloroacetyl‐CoA with rabbit fatty acid synthase

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