scholarly journals Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity

2017 ◽  
Vol 45 (10) ◽  
pp. 5863-5876 ◽  
Author(s):  
Ullas Valiya Chembazhi ◽  
Vinod Vikas Patil ◽  
Shivjee Sah ◽  
Wayne Reeve ◽  
Ravi P. Tiwari ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Dna Glycosylase ◽  
Uracil Dna Glycosylase ◽  
Broad Substrate Specificity ◽  
New Class

Characterization of GM-CSF-inhibitory factor and Uracil DNA glycosylase encoding genes from camel pseudocowpoxvirus

2015 ◽  
Vol 100 ◽  
pp. 291-296 ◽  
Author(s):  
G. Nagarajan ◽  
Shelesh Kumar Swami ◽  
Shyam Singh Dahiya ◽  
S.D. Narnaware ◽  
S.C. Mehta ◽  
...  
Keyword(s):  
Inhibitory Factor ◽  
Dna Glycosylase ◽  
Uracil Dna Glycosylase ◽  
Gm Csf ◽  
Encoding Genes

Characterization of cold-active uracil-DNA glycosylase from Bacillus sp. HJ171 and its use for contamination control in PCR

2008 ◽  
Vol 80 (5) ◽  
pp. 785-794 ◽  
Author(s):  
Gun A. Kim ◽  
Mi Sun Lee ◽  
Younguk Sun ◽  
Byung Doo Lee ◽  
Jong Il Lee ◽  
...  
Keyword(s):  
Dna Glycosylase ◽  
Bacillus Sp ◽  
Uracil Dna Glycosylase ◽  
Contamination Control ◽  
Cold Active

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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