The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064
Article Abstract:
The haloalkane dehalogenase (dhaA) gene from Rhodococcus rhodochrous NCIMB 13064 was cloned, sequenced and compared with the dhIA gene from Xanthobacter autotrophicus GJ10 from which, no sequence homology was found. The amino acid sequence of their gene products however, exhibited about 30% identity. The results of functional analysis revealed that Escherichia coli cells have a high level of expression of the dhaA gene which encode a dehalogenase that targets chloroalkanes of chain length C3-C10 and 1,2-dichloroethane. The findings also indicated that rearrangements of DNA in the dhaA may influence the control of expression of the enzyme in R. rhodochrous NCMIB 13064.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Long-chain haloalkanes are incorporated into fatty acids by Rhodococcus rhodochrous NCIMB 13064
Article Abstract:
The carbon chain length, the characteristics and the position of the halogen substituent in the haloalkane growth substrate affect the fatty acid composition of the cellular lipids of Rhodococcus rhodochrous NCIMB 13064 developed on several long-chain haloalkanes. Omega-chloro, -bromo and iodofatty acids incorporate in cellular lipids from C12 to C18 substrates at levels varying from 21% with C12 to 75% with C16. The incorporation of the haloacids is insensitive of the halogen position.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Identification of a phenolic 3-0-methyltransferase in the lignin-degrading fungus Phanerochaete chrysosporium
Article Abstract:
A methyltransferase enzyme catalysing the 3-O-methylation of isovanillic acid by S-adenosylmethionine (SAM) was identified in Phanerochaete chrysosporium. Purification and substrate utilization studies reveal that the enzyme was highly specific and displayed exclusive preference for the methylation of the 3-hydroxyl group of several substituted benzoic acids. Furthermore, the meta-specific enzyme was believed to have a role in the 4-o-methylation of lignin degradation products.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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