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.

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

Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Characterization ◽  
Side Chains ◽  
Amino Acid Residues

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.

scholarly journals Inside Cover: Synthesis and Structural Characterization of Homochiral Homo-oligomers of Parent cis- and trans-Furanoid-β-Amino Acids (Chem. Eur. J. 46/2011)

2011 ◽  
Vol 17 (46) ◽  
pp. 12834-12834
Author(s):  
Sunil K. Pandey ◽  
Ganesh F. Jogdand ◽  
João C. A. Oliveira ◽  
Ricardo A. Mata ◽  
Pattuparambil R. Rajamohanan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Structural Characterization ◽  
Cis And Trans

Synthesis and Structural Characterization of Homochiral Homo-Oligomers of cis-γ-Methoxy-Substituted cis- and trans-Furanoid-β-Amino Acids

2012 ◽  
Vol 2012 (13) ◽  
pp. 2656-2663 ◽  
Author(s):  
Awadut G. Giri ◽  
Ganesh F. Jogdand ◽  
Pattuparampil R. Rajamohanan ◽  
Sunil K. Pandey ◽  
Chepuri V. Ramana
Keyword(s):  
Amino Acids ◽  
Structural Characterization ◽  
Cis And Trans

scholarly journals UDP-sugar Pyrophosphorylase with Broad Substrate Specificity Toward Various Monosaccharide 1-Phosphates from Pea Sprouts

2004 ◽  
Vol 279 (44) ◽  
pp. 45728-45736 ◽  
Author(s):  
Toshihisa Kotake ◽  
Daisuke Yamaguchi ◽  
Hiroshi Ohzono ◽  
Sachiko Hojo ◽  
Satoshi Kaneko ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Substrate Specificity ◽  
Molecular Mass ◽  
Glucuronic Acid ◽  
De Novo ◽  
Higher Plants ◽  
Maximum Activity ◽  
Broad Substrate Specificity ◽  
Salvage Pathways

UDP-sugars, activated forms of monosaccharides, are synthesized throughde novoand salvage pathways and serve as substrates for the synthesis of polysaccharides, glycolipids, and glycoproteins in higher plants. A UDP-sugar pyrophosphorylase, designated PsUSP, was purified about 1,200-fold from pea (Pisum sativumL.) sprouts by conventional chromatography. The apparent molecular mass of the purified PsUSP was 67,000 Da. The enzyme catalyzed the formation of UDP-Glc, UDP-Gal, UDP-glucuronic acid, UDP-l-arabinose, and UDP-xylose from respective monosaccharide 1-phosphates in the presence of UTP as a co-substrate, indicating that the enzyme has broad substrate specificity toward monosaccharide 1-phosphates. Maximum activity of the enzyme occurred at pH 6.5–7.5, and at 45 °C in the presence of 2 mmMg2+. The apparentKmvalues for Glc 1-phosphate andl-arabinose 1-phosphate were 0.34 and 0.96 mm, respectively.PsUSPcDNA was cloned by reverse transcriptase-PCR.PsUSPappears to encode a protein with a molecular mass of 66,040 Da (600 amino acids) and possesses a uridine-binding site, which has also been found in a human UDP-N-acetylhexosamine pyrophosphorylase. Phylogenetic analysis revealed that PsUSP can be categorized in a group together with homologues fromArabidopsisand rice, which is distinct from the UDP-Glc and UDP-N-acetylhexosamine pyrophosphorylase groups. Recombinant PsUSP expressed inEscherichia colicatalyzed the formation of UDP-sugars from monosaccharide 1-phosphates and UTP with efficiency similar to that of the native enzyme. These results indicate that the enzyme is a novel type of UDP-sugar pyrophosphorylase, which catalyzes the formation of various UDP-sugars at the end of salvage pathways in higher plants.

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