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 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 Cloning, expression, and functional characterization of an organophosphates insecticides degrading gene (opdC) from a potential probiotic Lactobacillus plantarum WCP931

2020 ◽  
Author(s):  
Md. Azizul Haque ◽  
Hee Yul Lee ◽  
Du Yong Cho ◽  
Jin Hwan Lee ◽  
Chung Eun Hwang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Survival Rate ◽  
Substrate Specificity ◽  
Functional Characterization ◽  
Relative Activity ◽  
Maximum Activity ◽  
Significant Survival ◽  
Sds Page ◽  
Probiotic Lactobacillus

Abstract An organophosphorus (OP) insecticides degrading strain Lactobacillus plantarum WCP931, harboring OP hydrolase (OpdC) gene, was isolated during kimchi fermentation. The strain WCP931 appeared a significant survival rate of 51 to 96% under the artificial gastric acidic condition at pH 2 to 3 after 3 h. The opdC gene consisting 831 bp encoding 276 amino acids was cloned from the strain WCP907. The recombinant Escherischia coli harboring opdC gene depleted 77% chlorpyrifos (CP) in M9 medium after 6 days of incubation. The OpdC enzyme represents a novel member of GHSQG family of esterolytic enzymes or new Opd group. The OpdC molecular mass was estimated to be approximately 31 kDa in SDS-PAGE and showed maximum activity at 40 οC with pH 6. However, the mutated OpdC (Ser116 → Ala116) enzyme had no activity towards OP insecticides and ρ-nitrophenol-β-butyrate. Importantly, relative activity of OpdC against P-O bond insecticides was higher than P-S bond insecticide, which indicated its broad substrate specificity. It is suggested that opdC gene of strain WCP931 play role for the biodegradation of OP insecticides during kimchi fermentation.

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

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