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 …

The aim of the present review is to highlight the potential use of marine biocatalysts (whole
cells or enzymes) as an alternative bioprocess for the degradation of aromatic pollutants …

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 …

Ancestral sequence reconstruction (ASR) represents a powerful approach for empirical
testing structure‐function relationships of diverse proteins. We employed ASR to predict …

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

Haloalkane dehalogenase (HLD) enzymes employ an SN2 nucleophilic substitution
mechanism to erase halogen substituents in diverse organohalogen compounds. Subfamily …

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