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Inhibitory Activity of Alkoxyalkyl and Alkyl Esters of Cidofovir and Cyclic Cidofovir against Orthopoxvirus Replication In Vitro. Kathy A. Keith, 2004.A new series of ether lipid esters of cidofovir (CDV) were evaluated against vaccinia and cowpox viruses . Activity was dependent on number of atoms in the alkyl or alkoxyalkyl chain, the linker moiety, and the presence of a double bond in the alkoxyalkyl chains linked to the phosphonate moiety of CDV . In Vitro Laser Ablation of Natural Marine Biofilms. Kanavillil Nandakumar, 2004. Mycobacterium smegmatis L-Alanine Dehydrogenase (Ald) Is Required for Proficient Utilization of Alanine as a Sole Nitrogen Source and Sustained Anaerobic Growth. Zhengyu Feng, 2002.NAD(H)-dependent L-alanine dehydrogenase (EC 1.4.1.1) (Ald) catalyzes the oxidative deamination of L-alanine and the reductive amination of pyruvate . To assess the physiological role of Ald in Mycobacterium smegmatis, we cloned the ald gene, identified its promoter, determined the protein expression levels, and analyzed the combined effects of nutrient supplementation, oxygen availability, and growth stage on enzyme activity . High Ald activities were observed in cells grown in the presence of L- or D-alanine regardless of the oxygen availability and growth stage . In exponentially growing cells under aerobic conditions, supplementation with alanine resulted in a 25- to 50-fold increase in the enzyme activity . In the absence of alanine supplementation, 23-fold-higher Ald activities were observed in cells grown exponentially under anaerobic conditions . Furthermore, M . smegmatis ald null mutants were constructed by targeted disruption and were shown to lack any detectable Ald activity . In contrast, the glycine dehydrogenase (EC 1.4.1.10) (Gdh) activity in mutant cells remained at wild-type levels, indicating that another enzyme protein is responsible for the physiologically relevant reductive amination of glyoxylate . The ald mutants grew poorly in minimal medium with L-alanine as the sole nitrogen source, reaching a saturation density 100-fold less than that of the wild-type strain . Likewise, mutants grew to a saturation density 10-fold less than that of the wild-type strain under anaerobic conditions . In summary, the phenotypes displayed by the M . smegmatis ald mutants suggest that Ald plays an important role in both alanine utilization and anaerobic growth . Cel9M, a New Family 9 Cellulase of the Clostridium cellulolyticum Cellulosome. Anne Belaich, 2002.A new cellulosomal protein from Clostridium cellulolyticum Cel9M was characterized . The protein contains a catalytic domain belonging to family 9 and a dockerin domain . Cel9M is active on carboxymethyl cellulose, and the hydrolysis of this substrate is accompanied by a decrease in viscosity . Cel9M has a slight, albeit significant, activity on both Avicel and bacterial microcrystalline cellulose, and the main soluble sugar released is cellotetraose . Saccharification of bacterial microcrystalline cellulose by Cel9M in association with two other family 9 enzymes from C . cellulolyticum, namely, Cel9E and Cel9G, was measured, and it was found that Cel9M acts synergistically with Cel9E . Complexation of Cel9M with the mini-CipC1 containing the cellulose binding domain, the X2 domain, and the first cohesin domain of the scaffoldin CipC of the bacterium did not significantly increase the hydrolysis of Avicel and bacterial microcrystalline cellulose .
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