Phosphopantetheine transferase
Webtransferase (PPTase) interrogates the essential acyl carrier protein (ACP) domain to fulfill the initial activation step. The triggering factor of this study was the lack of structural information on PPTases at physiological pH, which could bias our comprehension of the mechanism of action of these important enzymes. WebThe structure of co-purified FAS shows discernible acyl carrier protein (ACP) domains and phosphopantetheine transferase (PPT) domains, which are responsible for substrate shuttling among ...
Phosphopantetheine transferase
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WebMay 1, 2001 · A single candidate 4'-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized. The human enzyme, which is ... WebJun 18, 2003 · A single candidate 4'-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized. The human enzyme, which is expressed mainly in the cytosolic compartment in a wide range of tissues, is a 329-residue, monomeric protein.
WebNational Center for Biotechnology Information WebA single candidate 4'-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized.
WebJul 1, 2001 · Chapter 10 using phosphopantetheinyl transferases for enzyme posttranslational activation, site specific protein labeling and identification of natural product biosynthetic gene clusters from bacterial genomes. Murat Sunbul, Keya Zhang, Jun Yin Biology, Chemistry Methods in enzymology 2009 24 View 2 excerpts, cites background WebFeb 15, 2009 · The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT) ...
Webphosphopantetheine transferase (PPTase), thus converting it to the active holoCP (3) (Fig. 1). Many organisms utilize more than one Ppant-dependent pathway. For instance, aside …
WebActivates the seven peptidyl carrier protein (PCP) domains of surfactin synthase SRF1/2/3 by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cells of B.subtilis to become producers of the lipopeptide antibiotics surfactin and plipastatin B1. Pfam Domain Function ACPS ( PF01648) reach registration searchPhosphopantetheine, also known as 4'-phosphopantetheine, is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). It is also present in formyltetrahydrofolate dehydrogenase. reach registrierte stoffeWebAlthough holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark … reach registration statusWebFeb 15, 2009 · The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT). reach registryWebJun 6, 2024 · Unique CFP (cysteine-free protein; 120 aa) has been identified as an extraordinary virulence factor in Beauveria bassiana (Cordycipitaceae), a main source of wide-spectrum fungal insecticides. Its homologs exclusively exist in wide-spectrum insect pathogens of Hypocreales, suggesting their importance for a fungal insect-pathogenic … reach registration requirementsWebJul 1, 2002 · 1 Introduction. 4′-Phosphopantetheinyl transferases (PPTases) catalyze the conversion of 4′-phosphopantetheine (Ppant)-dependent carrier proteins from their inactive apo- into the active holo-form [1, 2].In this reaction, the Ppant moiety is derived from coenzyme A and transferred onto the side chain β-hydroxyl group of a conserved serine … reach registration polymersWebAn object of the present invention is to provide a microorganism that efficiently produces EPA and a method for producing EPA using the microorganism. The present invention relates to a microorganism having an ability to produce docosahexaenoic acid (DHA), wherein the microorganism contains a protein composed of an amino acid sequence in … reach registry pad