Biochemical Characterization of a Novel Haloalkane Dehalogenase from a Cold-Adapted Bacterium
نویسندگان
چکیده
منابع مشابه
Biochemical Characterization of a Haloalkane Dehalogenase DadB from Alcanivorax dieselolei B-5
Recently, we found that Alcanivorax bacteria from various marine environments were capable of degrading halogenated alkanes. Genome sequencing of A. dieselolei B-5 revealed two putative haloalkane dehalogenase (HLD) genes, which were supposed to be involved in degradation of halogenated compounds. In this report, we confirm for the first time that the Alcanivorax bacterium encodes a truly funct...
متن کاملDiscovery of Novel Haloalkane Dehalogenase Inhibitors.
Haloalkane dehalogenases (HLDs) have recently been discovered in a number of bacteria, including symbionts and pathogens of both plants and humans. However, the biological roles of HLDs in these organisms are unclear. The development of efficient HLD inhibitors serving as molecular probes to explore their function would represent an important step toward a better understanding of these interest...
متن کاملBiochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58.
We report the biochemical characterization of a novel haloalkane dehalogenase, DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58. DatA possesses a peculiar pair of halide-stabilizing residues, Asn-Tyr, which have not been reported to play this role in other known haloalkane dehalogenases. DatA has a number of other unique characteristics, including substrate-dependent and coo...
متن کاملBiochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.
A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity....
متن کاملPurification and characterization of a novel cold adapted fungal glucoamylase
BACKGROUND Amylases are used in various industrial processes and a key requirement for the efficiency of these processes is the use of enzymes with high catalytic activity at ambient temperature. Unfortunately, most amylases isolated from bacteria and filamentous fungi have optimal activity above 45 °C and low pH. For example, the most commonly used industrial glucoamylases, a type of amylase t...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2012
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.00485-12