gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Malonyl CoA:ACP acyltransferase

The protein encoded by this gene is found exclusively in the mitochondrion, where it catalyzes the transfer of a malonyl group from malonyl-CoA to the mitochondrial acyl carrier protein. The encoded protein may be part of a fatty acid synthase complex that is more like the type II prokaryotic and plastid complexes rather than the type I human cytosolic complex. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: ACID, CAN, Actin, V1a, STEP
Papers on FABD
Functional replacement of the Saccharomyces cerevisiae fatty acid synthase with a bacterial type II system allows flexible product profiles.
Da Silva et al., Irvine, United States. In Biotechnol Bioeng, Dec 2015
The E. coli acpS + acpP (together), fabB, fabD, fabG, fabH, fabI, fabZ, and tesA were expressed in individual S. cerevisiae strains, and enzyme activity was confirmed by in vitro activity assays.
Regulating malonyl-CoA metabolism via synthetic antisense RNAs for enhanced biosynthesis of natural products.
Yan et al., Athens, United States. In Metab Eng, May 2015
The optimized asRNA constructs with a loop-stem structure exhibit high interference efficiency up to 80%, leading to a 4.5-fold increase in intracellular malonyl-CoA concentration when fabD gene expression is inhibited.
Effective qPCR methodology to quantify the expression of virulence genes in Aeromonas salmonicida subsp. salmonicida.
Farto et al., Vigo, Spain. In J Appl Microbiol, Apr 2015
The most stable reference genes were gyrB, proC and rpoC, while rpoD and fabD were the least stable.
Multivariate PLS Modeling of Apicomplexan FabD-Ligand Interaction Space for Mapping Target-Specific Chemical Space and Pharmacophore Fingerprints.
Surolia et al., Bengaluru, India. In Plos One, 2014
In this study, active site architecture of FabD drug target in two apicomplexan parasites viz.
Salmonella survival and differential expression of fatty acid biosynthesis-associated genes in a low-water-activity food.
Critzer et al., Knoxville, United States. In Lett Appl Microbiol, 2014
Correspondingly, gene expression was evaluated for three selected genes involved in fatty acid biosynthesis and modification (fabA, fabD and cfa).
A cis-encoded sRNA controls the expression of fabH2 in Yersinia.
Chen et al., Wuhan, China. In Febs Lett, 2014
Constitutive and inducible over-expression of YsrH decreased the mRNA level of fabH2, while expression of downstream fabD and fabG remained unaffected.
Survival of Salmonella enterica in poultry feed is strain dependent.
Hanning et al., Knoxville, United States. In Poult Sci, 2014
The purpose of this research was to compare the ability of Salmonella serovars and strains to survive in broiler feed and to evaluate molecular mechanisms associated with survival and colonization by measuring the expression of genes associated with colonization (hilA, invA) and survival via fatty acid synthesis (cfa, fabA, fabB, fabD).
Distinct functional domains of the Abelson tyrosine kinase control axon guidance responses to Netrin and Slit to regulate the assembly of neural circuits.
Bashaw et al., Philadelphia, United States. In Development, 2013
Moreover, we find that Abl exerts its diverse activities through at least two different mechanisms: (1) a partly kinase-independent, structural function in midline attraction through its C-terminal F-actin binding domain (FABD) and (2) a kinase-dependent inhibition of repulsive guidance pathways that does not require the Abl C terminus.
Cloning and functional analysis of putative malonyl-CoA:acyl-carrier protein transacylase gene from the docosahexaenoic acid-producer Schizochytrium sp. TIO1101.
Huang et al., Hangzhou, China. In World J Microbiol Biotechnol, 2013
In this study, the putative fabD gene coding MCAT was isolated from Schizochytrium sp.
Rv3080c regulates the rate of inhibition of mycobacteria by isoniazid through FabD.
Srivastava et al., Lucknow, India. In Mol Cell Biochem, 2013
The mycobacterial FASII multi-enzyme complex has been identified to be a target of Ser/Thr protein kinases (STPKs) of Mycobacterium tuberculosis (MTB), with substrates, including the malonyl-CoA:ACP transacylase (FabD) and the β-ketoacyl-ACP synthases KasA and KasB.
Identification and validation of reference genes to study the gene expression in Gluconacetobacter diazotrophicus grown in different carbon sources using RT-qPCR.
Simões-Araújo et al., Seropédica, Brazil. In J Microbiol Methods, 2012
To evaluate and identify suitable reference genes for gene expression normalization in the diazotrophic G. diazotrophicus, mRNA levels of fourteen candidate genes (rpoA, rpoC, recA, rpoD, fabD, gmk, recF, rho, ldhD, gyrB, gyrBC, dnaG, lpxC and 23SrRNA) and three target genes (matE, omp16 and sucA) were quantified by RT-qPCR after growing the bacteria in different carbon sources.
An analysis of the concentration change of intermediate metabolites by gene manipulation in fatty acid biosynthesis.
Won et al., Seoul, South Korea. In Enzyme Microb Technol, 2012
In this report, concentration of malonic acid and acetic acid produced in Escherichia coli were investigated by the expression of acetyl-CoA carboxylase genes (accs) and a malonyl-CoA:ACP transacylase gene (fabD).
Altered expression level of Escherichia coli proteins in response to treatment with the antifouling agent zosteric acid sodium salt.
Cappitelli et al., Milano, Italy. In Environ Microbiol, 2012
PptA, AroA, FabD, FabB, GapA) proteins.
Functional characterizations of malonyl-CoA:acyl carrier protein transacylase (MCAT) in Eimeria tenella.
Cai et al., Guangzhou, China. In Mol Biochem Parasitol, 2012
Malonyl-CoA:acyl-carry protein transacylase (MCAT) encoded by the fabD gene is one of the essential enzymes in the FAS II system.
Heterologous co-expression of accA, fabD, and thioesterase genes for improving long-chain fatty acid production in Pseudomonas aeruginosa and Escherichia coli.
Lee et al., Seoul, South Korea. In Appl Biochem Biotechnol, 2012
By introducing two genes (accA and fabD) of P. aeruginosa into the two bacterial strains and by co-expressing with them the fatty acyl-acyl carrier protein thioesterase gene of Streptococcus pyogenes (strain MGAS10270), we have engineered recombinant strains that are efficient producers of long-chain fatty acids (C16 and C18).
share on facebooktweetadd +1mail to friends