Selectivity of the Yersiniabactin Synthetase Adenylation Domain in the Two-Step Process of Amino Acid Activation and Transfer to a Holo-Carrier Protein Domain†

Biochemistry ◽  
2000 ◽  
Vol 39 (9) ◽  
pp. 2297-2306 ◽  
Author(s):  
Thomas A. Keating ◽  
Zucai Suo ◽  
David E. Ehmann ◽  
Christopher T. Walsh
Keyword(s):  
Amino Acid ◽  
Protein Domain ◽  
Carrier Protein ◽  
Acid Activation ◽  
Adenylation Domain ◽  
Step Process ◽  
Amino Acid Activation

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

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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