Amide compound synthesis by adenylation domain of bacillibactin synthetase
نویسندگان
چکیده
منابع مشابه
Yonus et al. Structure of the adenylation domain DltA 1 CRYSTAL STRUCTURE OF DLTA: IMPLICATIONS FOR THE REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE (NRPS) ADENYLATION DOMAINS*
Structure of the adenylation domain DltA 1 CRYSTAL STRUCTURE OF DLTA: IMPLICATIONS FOR THE REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE (NRPS) ADENYLATION DOMAINS* Huma Yonus, Piotr Neumann, Stephan Zimmermann, Jürgen J. May, Mohamed A. Marahiel and Milton T. Stubbs From the Institut für Biochemie und Biotechnologie, Martin-Luther-Universität HalleWittenberg, Kurt-Mothes-Straße 3, D-0...
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Threonyl-tRNA synthetase (ThrRS) must discriminate among closely related amino acids to maintain the fidelity of protein synthesis. Here, a pre-steady state kinetic analysis of the ThRS-catalyzed adenylation reaction was carried out by monitoring changes in intrinsic tryptophan fluorescence. Stopped flow fluorimetry for the forward reaction gave a saturable fluorescence quench whose apparent ra...
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BACKGROUND Nonribosomal peptide synthetases (NRPSs) are large modular proteins that selectively bind, activate and condense amino acids in an ordered manner. Substrate recognition and activation occurs by reaction with ATP within the adenylation (A) domain of each module. Recently, the crystal structure of the A domain from the gramicidin synthetase (GrsA) with L-phenylalanine and adenosine mon...
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We have examined three mutants of Klebsiella aerogenes whose genetic lesions (glnB, glnD, and glnE) are in loci unlinked to the structural gene for glutamine sythetase (glnA) and in which the control of both the level and state of adenylylation of glutamine synthetase is altered. Each mutation alters a different component of the adenylylation system of glutamine synthetase [L-glutamate:ammonia ...
متن کاملIdentification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
An improved method was developed to align related protein sequences and search for homology. A glutamine amide transfer domain was identified in an NH2-terminal segment of GMP synthetase from Escherichia coli. Amino acid residues 1-198 in GMP synthetase are homologous with the glutamine amide transfer domain in trpG X D-encoded anthranilate synthase component II-anthranilate phosphoribosyltrans...
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ژورنال
عنوان ژورنال: The Journal of Antibiotics
سال: 2016
ISSN: 0021-8820,1881-1469
DOI: 10.1038/ja.2016.117