Article Abstract:
The role of microbial esterases that have the ability to 'shave' some of the side chains and disrupt the cross-links of plant polymers in providing nutrients for saprophytic and pathogenic microorganisms was examined. While some esterases remove methoxyl side chains, thus enhancing the possibility of successful infection of plant tissue, others remove the groups which prevent access of the substrate to the active site resulting in the improvement of the rate at which main-chain-degrading enzymes hydrolyze the polysaccharide backbone.
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Article Abstract:
Sequence analysis of the esterase gene from Pseudomonas fluorescens reveals that 40-50% amino acids of the esterase are identical to those of the non-haem haloperoxidases. Esterase also exhibits functional homology to haloperoxidases. Esterase is a member of haloperoxidase family and is capable of performing halogenation as well as ester hydrolysis. Ser95, His252 and Asp223 constitute the catalytic triad in the esterase and the sequences of all bacterial non-haem haloperoxidases have a structurally similar catalytic triad.
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Article Abstract:
Spectinomycin (Sp) resistance genes in Streptomyces flavopersicus were isolated and analyzed to allow the investigation of Sp biosynsthesis. The plasmid vector pIJ699 was used to clone the Sp resistance determinant from S. flavopersicus into Streptomyces lividans. A pDGL15 plasmid, with a 3.65 kb insert from S. flavopersicus which was found to confer resistance to sp was isolated.
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