NRPSsp: non-ribosomal peptide synthase substrate predictor [PDF]
Bioinformatics, 2011 Abstract Summary: Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes, which biosynthesize many important peptide compounds produced by bacteria and fungi. Some studies have revealed that an individual domain within the NRPSs shows significant substrate selectivity.
Prieto, Carlos +3 more
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European Journal of Biochemistry, 1993 The amino acid sequence for the constitutive rat brain nitric oxide (NO) synthase was analysed by a set of computer programs that estimate and display physicochemical properties such as hydrophilicity, flexibility, accessibility, hydrophilic periodicity and conformation [Comerford, S. A., McCance, D. J., Dougan, G. & Tite, J. P. (1991) J. Virol. 65,
V, Riveros-Moreno +2 more
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The Janthinobacterium sp. HH01 genome encodes a homologue of the V. cholerae CqsA and L. pneumophila LqsA autoinducer synthases [PDF]
, 2013 Janthinobacteria commonly form biofilms on eukaryotic hosts and are known to synthesize antibacterial and antifungal compounds. Janthinobacterium sp. HH01 was recently isolated from an aquatic environment and its genome sequence was established.
Blokesch, Melanie +20 more
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Engineering polyketide synthases and nonribosomal peptide synthetases [PDF]
Current Opinion in Structural Biology, 2013 Naturally occurring polyketides and nonribosomal peptides with broad and potent biological activities continue to inspire the discovery of new and improved analogs. The biosynthetic apparatus responsible for the construction of these natural products has been the target of intensive protein engineering efforts. Traditionally, engineering has focused on
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The role of the phosphopantetheinyltransferase enzyme, PswP, in the biosynthesis of antimicrobial secondary metabolites by Serratia marcescens Db10 [PDF]
, 2014 Phosphopantetheinyltransferase (PPTase) enzymes fulfil essential roles in primary and secondary metabolism in prokaryotes, archaea and eukaryotes. PPTase enzymes catalyse the essential modification of the carrier protein domain of fatty acid synthases ...
Amy J. Gerc +9 more
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Thermodynamics of apocalmodulin and nitric oxide synthase II peptide interaction [PDF]
FEBS Letters, 2004 The Ca2+‐free form of calmodulin (CaM), apocalmodulin (ApoCaM), regulates a variety of target proteins including nitric oxide synthase II (NOS‐II). The CaM‐binding site of NOS‐II can bind ApoCaM with high affinity. Substitution of hydrophobic amino acids by charged amino acids at crucial positions 3, 9 and 13 within the CaM‐binding motif did not ...
Censarek, Petra +2 more
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Inhibition of Escherichia coli ATP synthase by amphibian antimicrobial peptides [PDF]
International Journal of Biological Macromolecules, 2010 Previously melittin, the alpha-helical basic honey bee venom peptide, was shown to inhibit F(1)-ATPase by binding at the beta-subunit DELSEED motif of F(1)F(o)-ATP synthase. Herein, we present the inhibitory effects of the basic alpha-helical amphibian antimicrobial peptides, ascaphin-8, aurein 2.2, aurein 2.3, carein 1.8, carein 1.9, citropin 1.1 ...
Laughlin, Thomas F., Ahmad, Zulfiqar
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De novo formation of an aggregation pheromone precursor by an isoprenyl diphosphate synthase-related terpene synthase in the harlequin bug. [PDF]
, 2018 Insects use a diverse array of specialized terpene metabolites as pheromones in intraspecific interactions. In contrast to plants and microbes, which employ enzymes called terpene synthases (TPSs) to synthesize terpene metabolites, limited information ...
Ghosh, Saikat Kumar B +17 more
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Molecular biology of natriuretic peptides and nitric oxide synthases [PDF]
Cardiovascular Research, 2001 Natriuretic peptides and nitric oxide play important roles in cardiovascular and renal physiology and disease. The natriuretic peptides - atrial natriuretic peptide, brain natriuretic peptide, and C-type natriuretic peptide - comprise a family of proteins that participate in the integrated control of intravascular volume and arterial blood pressure ...
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Soybean ENOD40 encodes two peptides that bind to sucrose synthase [PDF]
Proceedings of the National Academy of Sciences, 2002 ENOD40 is expressed at an early stage in root nodule organogenesis in legumes. Identification of ENOD40 homologs in nonleguminous plants suggests that this gene may have a more general biological function.
Röhrig, H. +4 more
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