scholarly journals Biochemical Characterization of a Carboxylesterase from the Archaeon Pyrobaculum sp. 1860 and a Rational Explanation of Its Substrate Specificity and Thermostability

2014 ◽  
Vol 15 (9) ◽  
pp. 16885-16910 ◽  
Author(s):  
Hua Shao ◽  
Li Xu ◽  
Yunjun Yan
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Rational Explanation

scholarly journals Biochemical Characterization of the DNA Substrate Specificity of Werner Syndrome Helicase

2002 ◽  
Vol 277 (26) ◽  
pp. 23236-23245 ◽  
Author(s):  
Robert M. Brosh ◽  
Juwaria Waheed ◽  
Joshua A. Sommers
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Werner Syndrome ◽  
Dna Substrate

scholarly journals Origin and evolution of transporter substrate specificity within the NPF family

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Morten Egevang Jørgensen ◽  
Deyang Xu ◽  
Christoph Crocoll ◽  
Heidi Asschenfeldt Ernst ◽  
David Ramírez ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Biosynthetic Pathways ◽  
Cyanogenic Glucosides ◽  
Evolutionary Path ◽  
Substrate Specificities ◽  
Origin And Evolution ◽  
Glucosinolate Biosynthesis ◽  
Phylogenetic Lineage

Despite vast diversity in metabolites and the matching substrate specificity of their transporters, little is known about how evolution of transporter substrate specificities is linked to emergence of substrates via evolution of biosynthetic pathways. Transporter specificity towards the recently evolved glucosinolates characteristic of Brassicales is shown to evolve prior to emergence of glucosinolate biosynthesis. Furthermore, we show that glucosinolate transporters belonging to the ubiquitous NRT1/PTR FAMILY (NPF) likely evolved from transporters of the ancestral cyanogenic glucosides found across more than 2500 species outside of the Brassicales. Biochemical characterization of orthologs along the phylogenetic lineage from cassava to A. thaliana, suggests that alterations in the electrogenicity of the transporters accompanied changes in substrate specificity. Linking the evolutionary path of transporter substrate specificities to that of the biosynthetic pathways, exemplify how transporter substrate specificities originate and evolve as new biosynthesis pathways emerge.

Molecular Cloning and Biochemical Characterization of VIM-12, a Novel Hybrid VIM-1/VIM-2 Metallo-β-lactamase from aKlebsiella pneumoniaeClinical Isolate, Reveal Atypical Substrate Specificity†

Biochemistry ◽  
2007 ◽  
Vol 46 (45) ◽  
pp. 13170-13178 ◽  
Author(s):  
Maria Kontou ◽  
Spyros Pournaras ◽  
Ioulia Kristo ◽  
Alexandros Ikonomidis ◽  
Antonios N. Maniatis ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Molecular Cloning ◽  
Biochemical Characterization

scholarly journals Biochemical Characterization of the POM-1 Metallo-β-Lactamase from Pseudomonas otitidis

2014 ◽  
Vol 59 (3) ◽  
pp. 1755-1758 ◽  
Author(s):  
Luisa Borgianni ◽  
Filomena De Luca ◽  
Maria Cristina Thaller ◽  
Yunsop Chong ◽  
Gian Maria Rossolini ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Functional Analysis ◽  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Content Type ◽  
Broad Substrate Specificity ◽  
Catalytic Activities

ABSTRACTThe POM-1 metallo-β-lactamase is a subclass B3 resident enzyme produced byPseudomonas otitidis, a pathogen causing otic infections. The enzyme was overproduced inEscherichia coliBL21(DE3), purified by chromatography, and subjected to structural and functional analysis. The purified POM-1 is a tetrameric enzyme of broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins.

scholarly journals Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases

FEBS Journal ◽  
2015 ◽  
Vol 282 (6) ◽  
pp. 1031-1042 ◽  
Author(s):  
Hanna-Kirsti S. Leiros ◽  
Kine Susann Waade Edvardsen ◽  
Gro Elin Kjaereng Bjerga ◽  
Ørjan Samuelsen
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization

scholarly journals A Haloalkane Dehalogenase from a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity

2017 ◽  
Vol 84 (2) ◽  
Author(s):  
Tomas Buryska ◽  
Petra Babkova ◽  
Ondrej Vavra ◽  
Jiri Damborsky ◽  
Zbynek Prokop
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Biochemical Characterization ◽  
Environmental Pollutants ◽  
Haloalkane Dehalogenase ◽  
Broad Substrate Specificity ◽  
Organic Cosolvents ◽  
Marine Metagenome ◽  
Ph Range

ABSTRACTThe haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to those of previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to having this unique substrate specificity, the enzyme was highly tolerant to organic cosolvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high overexpression yield (200 mg of protein per liter of cultivation medium; 50% of total protein), good tolerance to organic cosolvents, and a broad pH range make DmmA an attractive biocatalyst for various biotechnological applications.IMPORTANCEWe present a thorough biochemical characterization of the haloalkane dehalogenase DmmA from a marine metagenome. This enzyme with an unusually large active site shows remarkably broad substrate specificity, high overexpression, significant tolerance to organic cosolvents, and activity under a broad range of pH conditions. DmmA is an attractive catalyst for sustainable biotechnology applications, e.g., biocatalysis, biosensing, and biodegradation of halogenated pollutants. We also report its ability to convert multiple halogenated compounds to corresponding polyalcohols.

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