Amino acid activation and polymerization at modular multienzymes in nonribosomal peptide biosynthesis

Amino Acids ◽  
1996 ◽  
Vol 10 (3) ◽  
pp. 201-227 ◽  
Author(s):  
T. Stein ◽  
J. Vater
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Nonribosomal Peptide ◽  
Amino Acid Activation ◽  
Peptide Biosynthesis

scholarly journals Streptogramin B biosynthesis in Streptomyces pristinaespiralis and Streptomyces virginiae: molecular characterization of the last structural peptide synthetase gene.

1997 ◽  
Vol 41 (9) ◽  
pp. 1904-1909 ◽  
Author(s):  
V de Crécy-Lagard ◽  
W Saurin ◽  
D Thibaut ◽  
P Gil ◽  
L Naudin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Activation Domains ◽  
Amino Acid Activation ◽  
Streptomyces Virginiae ◽  
Streptomyces Pristinaespiralis ◽  
Degenerate Oligonucleotide ◽  
Peptide Synthetase ◽  
Different Origins

Streptomyces pristinaespiralis and S. virginiae both produce closely related hexadepsipeptide antibiotics of the streptogramin B family. Pristinamycins I and virginiamycins S differ only in the fifth incorporated precursor, di(mono)methylated amine and phenylalanine, respectively. By using degenerate oligonucleotide probes derived from internal sequences of the purified S. pristinaespiralis SnbD and SnbE proteins, the genes from two streptogramin B producers, S. pristinaespiralis and S. virginiae, encoding the peptide synthetase involved in the activation and incorporation of the last four precursors (proline, 4-dimethylparaaminophenylalanine [for pristinamycin I(A)] or phenylalanine [for virginiamycin S], pipecolic acid, and phenylglycine) were cloned. Analysis of the sequence revealed that SnbD and SnbE are encoded by a unique snbDE gene. SnbDE (4,849 amino acids [aa]) contains four amino acid activation domains, four condensation domains, an N-methylation domain, and a C-terminal thioesterase domain. Comparison of the sequences of 55 amino acid-activating modules from different origins confirmed that these sequences contain enough information for the performance of legitimate predictions of their substrate specificity. Partial sequencing (1,993 aa) of the SnbDE protein of S. virginiae allowed comparison of the proline and aromatic acid activation domains of the two species and the identification of coupled frameshift mutations.

scholarly journals The Mechanism of Amino Acid Activation: the Work of Mahlon Hoagland

2009 ◽  
Vol 284 (25) ◽  
pp. e7-e8
Author(s):  
Nicole Kresge ◽  
Robert D. Simoni ◽  
Robert L. Hill
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Amino Acid Activation

scholarly journals The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis

2001 ◽  
Vol 14 (3) ◽  
pp. 336-348 ◽  
Author(s):  
Brenda K. Scholz-Schroeder ◽  
Michael L. Hutchison ◽  
Ingeborg Grgurina ◽  
Dennis C. Gross
Keyword(s):  
Pseudomonas Syringae ◽  
High Performance ◽  
Sweet Cherry ◽  
Peptide Structure ◽  
Acid Activation ◽  
Virulence Determinants ◽  
Amino Acid Activation ◽  
Peptide Synthetases ◽  
Peptide Synthetase ◽  
Peptide Biosynthesis

Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this module indicates that it incorporates 2,3-dehydroaminobutyric acid into the syringopeptin peptide structure. Bioassay and high performance liquid chromatography data confirmed that disruption of the sypA gene in strain B301D resulted in the loss of syringopeptin production. The contribution of syringopeptin and syringomycin to the virulence of P. syringae pv. syringae strain B301D was examined in immature sweet cherry with sypA and syrB1 synthetase mutants defective in the production of the two toxins, respectively. Syringopeptin (sypA) and syringomycin (syrB1) mutants were reduced in virulence 59 and 26%, respectively, compared with the parental strain in cherry, whereas the syringopeptin-syringomycin double mutant was reduced 76% in virulence. These data demonstrate that syringopeptin and syringomycin are major virulence determinants of P. syringae pv. syringae.

Amino-Acid Activation in Tissues of Early Embryos

Nature ◽  
1961 ◽  
Vol 191 (4792) ◽  
pp. 1006-1007 ◽  
Author(s):  
ELIZABETH M. DEUCHAR
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Amino Acid Activation ◽  
Early Embryos

scholarly journals Use of a spectrophotometric assay to evaluate amino acid activation and tRNA charging

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Japheth Mobisa ◽  
Kyra Samuel ◽  
Idiuso Okeke ◽  
Jacquelyn Castaneda ◽  
Thanh Trinh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Spectrophotometric Assay ◽  
Acid Activation ◽  
Amino Acid Activation

scholarly journals Differences in Amino Acid Activation Found Between Dwarf and Non Dwarf White Leghorn Chickens

1972 ◽  
Vol 51 (3) ◽  
pp. 1067-1068 ◽  
Author(s):  
R.G. Brown ◽  
A.S. Wood ◽  
B.S. Reinhart ◽  
D. Longworth
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
White Leghorn ◽  
Amino Acid Activation
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