scholarly journals Investigation of the Substrate Specificity of Lacticin 481 Synthetase by Using Nonproteinogenic Amino Acids

ChemBioChem ◽  
2009 ◽  
Vol 10 (5) ◽  
pp. 911-919 ◽  
Author(s):  
Matthew R. Levengood ◽  
Christopher C. Kerwood ◽  
Champak Chatterjee ◽  
Wilfred A. van der Donk
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Lacticin 481 ◽  
Lacticin 481 Synthetase

Cover Picture: Investigation of the Substrate Specificity of Lacticin 481 Synthetase by Using Nonproteinogenic Amino Acids (ChemBioChem 5/2009)

ChemBioChem ◽  
2009 ◽  
Vol 10 (5) ◽  
pp. 773-773
Author(s):  
Matthew R. Levengood ◽  
Christopher C. Kerwood ◽  
Champak Chatterjee ◽  
Wilfred A. van der Donk
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Lacticin 481 ◽  
Lacticin 481 Synthetase

scholarly journals On the Substrate Specificity of Dehydration by Lacticin 481 Synthetase

2007 ◽  
Vol 129 (8) ◽  
pp. 2212-2213 ◽  
Author(s):  
Xingang Zhang ◽  
Wilfred A. van der Donk
Keyword(s):  
Substrate Specificity ◽  
Lacticin 481 ◽  
Lacticin 481 Synthetase

scholarly journals Engineering Dehydro Amino Acids and Thioethers into Peptides Using Lacticin 481 Synthetase

2006 ◽  
Vol 13 (10) ◽  
pp. 1109-1117 ◽  
Author(s):  
Champak Chatterjee ◽  
Gregory C. Patton ◽  
Lisa Cooper ◽  
Moushumi Paul ◽  
Wilfred A. van der Donk
Keyword(s):  
Amino Acids ◽  
Lacticin 481 ◽  
Lacticin 481 Synthetase

scholarly journals The Leader Peptide Is Not Required for Post-Translational Modification by Lacticin 481 Synthetase

2007 ◽  
Vol 129 (34) ◽  
pp. 10314-10315 ◽  
Author(s):  
Matthew R. Levengood ◽  
Gregory C. Patton ◽  
Wilfred A. van der Donk
Keyword(s):  
Leader Peptide ◽  
Post Translational Modification ◽  
Lacticin 481 ◽  
Lacticin 481 Synthetase

scholarly journals Characterization of the Amino Acids fromNeisseria meningitidisMethionine Sulfoxide Reductase B Involved in the Chemical Catalysis and Substrate Specificity of the Reductase Step

2007 ◽  
Vol 282 (44) ◽  
pp. 32397-32405 ◽  
Author(s):  
Fabrice Neiers ◽  
Sanjiv Sonkaria ◽  
Alexandre Olry ◽  
Sandrine Boschi-Muller ◽  
Guy Branlant
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Chemical Catalysis

scholarly journals Mutants of the Zinc Ligands of Lacticin 481 Synthetase Retain Dehydration Activity but Have Impaired Cyclization Activity†

Biochemistry ◽  
2007 ◽  
Vol 46 (21) ◽  
pp. 6268-6276 ◽  
Author(s):  
Moushumi Paul ◽  
Gregory C. Patton ◽  
Wilfred A. van der Donk
Keyword(s):  
Lacticin 481 ◽  
Lacticin 481 Synthetase

Modulating substrate specificity of histone acetyltransferase with unnatural amino acids

2011 ◽  
Vol 7 (11) ◽  
pp. 3050 ◽  
Author(s):  
Kinjal Rajesh Mehta ◽  
Ching Yao Yang ◽  
Jin Kim Montclare
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Unnatural Amino Acids ◽  
Histone Acetyltransferase

scholarly journals Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis

2019 ◽  
Vol 75 (4) ◽  
pp. 299-306
Author(s):  
Jolanta Cieślak ◽  
Akimasa Miyanaga ◽  
Makoto Takaishi ◽  
Fumitaka Kudo ◽  
Tadashi Eguchi
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Natural Product ◽  
Structural Characterization ◽  
Biochemical Analysis ◽  
Natural Product Biosynthesis ◽  
Broad Substrate Specificity ◽  
Selective Incorporation ◽  
Polyketide Antibiotic

Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5′-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.

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