The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
substrate selectivity of the recombinant DhbF. Comparative mass spectrometric analysis of culture extracts from both the wild-type DhbF and the dhbF knockout mutant leads to the identification of a cyclic trimeric ester of DHB-glycine-threonine. Enzyme activity assay by ATP-diphosphate exchange reaction. For the DhbF1-A-PCP construct, a low but specific glycine-dependent ATP-diphosphate exchange is observed. For the second module, DhbF2-A-PCP, a highly specific ATP-diphosphate exchange dependent on L-threonine is observed. D-Threonine is not recognized as a substrate, whereas the stereoisomeric L-allo-Thr covers 47% activity
Mycobacterium tuberculosis SigM positively regulates Esx secreted protein and nonribosomal peptide synthetase genes and down regulates virulence-associated surface lipid synthesis.
the sfmB mutant strain TL2003 completely loses its ability to produce SFM-A, which is restored by expressing sfmB in trans, confirming the essential role of this NRPS system for SFM-A biosynthesis
the sfmB mutant strain TL2003 completely loses its ability to produce SFM-A, which is restored by expressing sfmB in trans, confirming the essential role of this NRPS system for SFM-A biosynthesis
Bacillus subtilis produces the catecholic siderophore itoic acid (2,3-dihydroxybenzoate (DHB)-glycine) in response to iron deprivation. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase. DhbF specifically adenylates threonine and, to a lesser extent, glycine and that covalently loads both amino acids onto their corresponding peptidyl carrier domains. The function of the terminal thioesterase domain (DhbF-Te) is to catalyze the intermolecular condensation of three DHB-Gly-Thr units and to release bacillibactin by intramolecular condensation. Mass spectrometric analysis, overview. Model for the assembly of bacillibactin
enzyme DhbF is involved in the addition of glycine to the siderophore 2,3-dihydroxybenzoate (DHB). Under iron-limiting conditions, Bacillus subtilis produces DHB to acquire extracellular iron
the enzyme is involved in the synthesis of saframycin A (SFM-A) by Streptomyces lavendulae strain NRRL 11002. The compound belongs to the tetrahydroisoquinoline family of antibiotics. The backbone of SFM-A is derived from one Ala, one Gly, and two Tyr residues, suggesting that it is of tetrapeptide origin. SfmA, SfmB, and SfmC constitute an NRPS system
Bacillus subtilis produces the catecholic siderophore itoic acid (2,3-dihydroxybenzoate (DHB)-glycine) in response to iron deprivation. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase. DhbF specifically adenylates threonine and, to a lesser extent, glycine and that covalently loads both amino acids onto their corresponding peptidyl carrier domains. The function of the terminal thioesterase domain (DhbF-Te) is to catalyze the intermolecular condensation of three DHB-Gly-Thr units and to release bacillibactin by intramolecular condensation. Mass spectrometric analysis, overview. Model for the assembly of bacillibactin
enzyme DhbF is involved in the addition of glycine to the siderophore 2,3-dihydroxybenzoate (DHB). Under iron-limiting conditions, Bacillus subtilis produces DHB to acquire extracellular iron
the enzyme is involved in the synthesis of saframycin A (SFM-A) by Streptomyces lavendulae strain NRRL 11002. The compound belongs to the tetrahydroisoquinoline family of antibiotics. The backbone of SFM-A is derived from one Ala, one Gly, and two Tyr residues, suggesting that it is of tetrapeptide origin. SfmA, SfmB, and SfmC constitute an NRPS system
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis revealed 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. The results of substrate prediction and in vitro characterization of the adenylation specificities of this NRPS system support the hypothesis that the last module acts in an iterative manner to form a tetrapeptidyl intermediate and that the co-linearity rule does not apply
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis revealed 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. The results of substrate prediction and in vitro characterization of the adenylation specificities of this NRPS system support the hypothesis that the last module acts in an iterative manner to form a tetrapeptidyl intermediate and that the co-linearity rule does not apply
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
generation of a dhbF gene disruption mutant generated from Bacillus subtilis strain ATCC 21332, integration and the double crossover event in the resulting Bacillus subtilis strain JJM405
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme DhbF, and separate DhbF modules DhbF1-A-PCP and DhbF2-A-PCP, from Escherichia coli strain BL21 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dhbF, DNA and amino acid sequence determination and analysis. By inspecting the DNA sequences of the genes dhbE, dhbB, and dhbF as annotated by the Bacillus subtilis genome project to encode the synthetase complex for the siderophore assembly, various sequence errors within the dhbF gene are predicted and confirmed by re-sequencing. According to the corrected sequence, dhbF encodes a dimodular instead of a monomodular nonribosomal peptide synthetase, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21, the separate DhbF modules DhbF1-A-PCP and DhbF2-A-PCP are also produced as individual proteins
gene dhbF, genetic organization of the Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes, cloning from a Bacillus subtilis YAC library, DNA and amino acid sequence determination and analysis, the dhb genes are located near 291° on the Bacillus subtilis chromosome
the biosynthetic gene cluster for SFM-A is cloned and localized to a 62-kb contiguous DNA region. Sequence analysis reveals 30 genes that constitute the SFM-A gene cluster, encoding an unusual nonribosomal peptide synthetase (NRPS) system and tailoring enzymes and regulatory and resistance proteins. Three NRPS genes, sfmA, sfmB and sfmC, are identified within the sfm cluster. Cloning of gene sfmB, part of the SFM-A gene cluster, DNA and amino acid sequence determination and analysis, genetic organization, recombinant expression in Pseudomonas fluorescens
Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin