Requirement of carbon dioxide for initial growth of facultative methylotroph, Acidomonas methanolica MB58.

The facultative methylotrophic bacterium Acidomonas methanolica MB58 can utilize C1 compounds via the ribulose monophosphate pathway. A large gene cluster comprising three components related to C1 metabolism was found in the genome. From upstream, the first was an mxa cluster encoding proteins for oxidation of methanol to formaldehyde; the second was the rmp cluster encoding enzymes for formaldehyde fixation; and the third was the cbb gene cluster encoding proteins for carbon dioxide (CO2) fixation.

Purification and characterization of vanillin dehydrogenases from alkaliphile Micrococcus sp. TA1 and neutrophile Burkholderia cepacia TM1.

Vanillin dehydrogenases (VDHs) were purified and characterized from two bacterial strains that have different pH dependencies for growth. The alkaliphile Micrococcus sp. TA1, isolated from an alkaline spa, can grow on several aromatic compounds such as ferulic acid, vanillin, vanillic acid, and protocatechuic acid under alkaline conditions.

Site-specific and asymmetric hydrolysis of prochiral 2-phenyl-1,3-propanediol diacetate by a bacterial esterase from an isolated strain.

Bacillus cereus 809A and Burkholderia sp. 711C were isolated from soil. These strains demonstrate hydrolysis activity towards prochiral 2-phenyl-1,3-propanediol diacetate and accumulated the corresponding chiral monoacetates into the reaction mixture.

Production of sepedonin by Sepedonium chrysospermum NT-1 in submerged culture.

Strains of Sepedonium chrysospermum and the anamorph strain of Hypomyces chrysospermus (congruent with Apiocrea chrysosperma) were isolated and purified from parasitic filamentous fungi on the fruiting bodies of Boletaceae, such as the Gyroponus and Suillus genera in Japan, and identified from formations of conidia and chlamydospores. It is known that these strains produce sepedonin. S.

Formaldehyde uptake by Methylobacterium sp. MF1 and Acidomonas methanolica MB 58 with the different formaldehyde assimilation pathways.

Methylobacterium sp. MF1 (an obligate methylotrophic bacterium isolated newly by the authors) and Acidomonas methanolica MB58 (a facultative methylotrophic bacterium) uptake formaldehyde similarly. It was found that the former assimilated formaldehyde via the serine pathway whereas the latter did so via the ribulose-monophosphate pathway from the measurement of the key enzyme activities in each assimilation pathway.

Thermolabile variant, PHOX-S, of prophenol oxidase in Drosophila melanogaster.

The Phox(S) strain of Drosophila melanogaster is an electrophoretically slow variant found in a wild population at Victoria, Australia. Prophenol oxidase isoform A(1) from PHOX-S was purified and characterized biochemically and genetically. The purified fraction of A(1) from PHOX-S showed a homodimer with a molecular weight of the subunit of approximately 77 kDa.

Formaldehyde-limited cultivation of a newly isolated methylotrophic bacterium, Methylobacterium sp. MF1: enzymatic analysis related to C1 metabolism.

Formaldehyde is a highly toxic compound to most living organisms. We have isolated a bacterial strain that is able to efficiently degrade formaldehyde and use it as a sole carbon source. The isolated strain was identified as Methylobacterium sp.

Formaldehyde fixation contributes to detoxification for growth of a nonmethylotroph, Burkholderia cepacia TM1, on vanillic acid.

During bacterial degradation of methoxylated lignin monomers, such as vanillin and vanillic acid, formaldehyde is released through the reaction catalyzed by vanillic acid demethylase. When Burkholderia cepacia TM1 was grown on vanillin or vanillic acid as the sole carbon source, the enzymes 3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexuloisomerase (PHI) were induced. These enzymes were also expressed during growth on Luria-Bertani medium containing formaldehyde.

E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A).

The inhibitory properties of TIMP-4 for matrix metalloproteinases (MMPs) were compared to those of TIMP-1 and TIMP-2. Full-length human TIMP-4 was expressed in E. coli, folded from inclusion bodies, and the active component was purified by MMP-1 affinity chromatography.