Abstract Haloalkane dehalogenases (EC 3.8. 1.5, HLDs) are α/β‐hydrolases which act to
cleave carbon‐halogen bonds. Due to their unique catalytic mechanism, broad substrate …

Haloalkane dehalogenases (HLDs) convert halogenated compounds to corresponding
alcohols, halides, and protons. They belong to α/β-hydrolases, and their principal catalytic …

Millions of protein sequences are being discovered at an incredible pace, representing an
inexhaustible source of biocatalysts. Here, we describe an integrated system for automated …

An enzyme's substrate specificity is one of its most important characteristics. The quantitative
comparison of broad-specificity enzymes requires the selection of a homogenous set of …

Haloalkane dehalogenases (HLDs) are enzymes that catalyze the cleavage of carbon–
halogen bonds by a hydrolytic mechanism. Although comparative biochemical analyses …

Next-generation sequencing doubles genomic databases every 2.5 years. The
accumulation of sequence data provides a unique opportunity to identify interesting …

Owing to the more abundant occurrence of racemic compounds compared to prochiral or
meso forms, most enantiomerically pure products are obtained via racemate resolution. This …

Recently, we found that Alcanivorax bacteria from various marine environments were
capable of degrading halogenated alkanes. Genome sequencing of A. dieselolei B-5 …

DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the
metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected …

Functional annotation of novel proteins lags behind the number of sequences discovered by
the next-generation sequencing. The throughput of conventional testing methods is far too …