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Bacillus subtilisgenesiolG,iolW,iolX,ntdC,yfiI,yrbE,yteT, andyulFbelong to the Gfo/Idh/MocA family. The functions ofiolG,iolW,iolX, andntdCare known; however, the functions of the others are unknown. We previously reported theB. subtiliscell factory simultaneously overexpressingiolGandiolWto achieve bioconversion ofmyo-inositol (MI) intoscyllo-inositol (SI). YulF shares a significant similarity with IolW, the NADP+-dependent SI dehydrogenase. Transcriptional abundance ofyulFdid not correlate to that ofiolgenes involved in inositol metabolism. However, whenyulFwas overexpressed instead ofiolWin theB. subtiliscell factory, SI was produced from MI, suggesting a similar function toiolW. In addition, we demonstrated that recombinant His6-tagged YulF convertedscyllo-inosose into SI in an NADPH-dependent manner. We have thus identifiedyulFencoding an additional NADP+-dependent SI dehydrogenase, which we propose to renameiolU. Among the Gfo/Idh/MocA family paralogs inB. subtilis, IolU turned out to be an additionalscyllo-inositol dehydrogenase. [ABSTRACT FROM AUTHOR]

The article presents a study concerning Bacillus subtilis FP-133 in relation to molecular cloning and sequence analysis of two distinct halotolerant extracellular proteases. It mentions that the study involves genes encoding of two distinct halotolerant extracellular proteases of Bacillus subtilis which are neutral proteases and alkaline serine. It shows that polar amino acid and acidic residues are located on the surface stabilize protein structure.

The 4-amino-3-hydroxybenzoate-assimilating Bordetella sp. strain 10d produces a deaminase that catalyzes the deamination of 2-amino-5-carboxymuconic 6-semialdehyde. A gene encoding the deaminase, ahdB, was cloned and expressed in Escherichia coli; ahdB is located downstream from the previously reported genes encoding 4-amino-3-hydroxybenzoate 2,3-dioxygenase ( ahdA) and a LysR-type regulator. The deduced amino acid sequence of ahdB shows 30–33% identity to those of previously reported 2-aminomuconate deaminases. We identified a region (RAGDFLXVSG) conserved in AhdB and three other deaminases. The recombinant enzyme AhdB was purified to homogeneity. After a coupled enzyme assay with purified AhdA, AhdB, and the substrate 4-amino-3-hydroxybenzoate, the final product, formed by the action of AhdA, AhdB, and by nonenzymatic decarboxylation, was identified by HPLC, MS, and 1H-nuclear magnetic resonance analyses as 2-hydroxymuconic 6-semialdehyde. [ABSTRACT FROM AUTHOR]

The article presents a study which focuses on the purification and characterization of an extracellular laccase enzyme from Phlebia radiate Strain BP-11-2. It mentions that this laccase was found in an isolated strain that has the capacity to decolorize fungal melanin. The study reveals that the enzyme has no absorption maximum in the ultraviolet region above 300 nanometer. In addition , it is different from any other laccases in terms of substrate specificity and kinetic parameters.

The article describes the purification of two alkaline, thermotolerant α-amylases from Bacillus halodurans 38C-2-1. The authors reveal that α-amylase I and II demonstrated maximal activities at 50-60°C and a pH of 10-11, and 38% relative activities at 30°C. They also discuss the production of AmyI, a cloned gene of α-amylase I, with a signal peptide.

The article discusses the study on the 4-amino-3-hydroxybenzoate metabolism, through Bordetella. The study involves the purification and characterization of enzymes. It has been inferred that the proposed metabolic pathway differs considerably from the modified meta-cleavage pathway of 2-aminophenol and those previously reported for methyl-and chloro-derivatives. Key information regarding the study are further discussed.

The article focuses on the purgation and depiction of two novel halotolerant extracellular proteases from Bacillus subtilis Strain FP-133. At a concentration of NaCl, both proteases opted animal proteins to vegetable proteins as natural substrates. In summation, under saline conditions, both proteases exhibited high catalytic activity toward gelatin and casein respectively.

cis,cis-Muconate cycloisomerase (MC) was purified to homogeneity from benzamide-assimilating Arthrobacter sp. BA-5-17. The purified enzyme showed high activities for cis,cis-muconate and 3-methyl-cis,cis-muconate, and preferred the 3-substituted derivatives over the derivatives with the same substituent at the 2 position as a substrate. A gene encoding MC of strain BA-5-17 was cloned and named catB. The catB gene was clustered with catR encoding a putative LysR-type regulator, catC encoding a putative muconolactone isomerase, and catA-II encoding the catechol 1,2-dioxygenase isozymes CD-III-1 and III-2. These genes showed the same orientation in transcriptional direction and the organization of cloned genes was catRBCA-II. In the phylogenetic analysis of MCs and chloro-MCs, the BA-5-17 and Streptomyces setonii MCs formed a subfamily, clearly distinguished from those of other MCs. [Copyright &y& Elsevier]

Analyzes the cloning and function of genes encoding an aniline dioxygenase of Frateuria Species ANA-18. Comparison between the constructions of the gene cluster and Pseudomonas tdn and Acinetobacter atd gene clusters; Observations on gene activity upon cloning; Function of the cloned tdn genes.

Reveals the regulatory mechanisms of the synthesis of enzymes involved in 2-aminophenol metabolism, compared to those enzymes involved in benzoate, p-Hydroxybenzoate, and protocatechuate metabolism in Pseudomonas sp. strain AP-3. Dioxygenase activities of the enzymes catalyzing the fission of benzene ring in cell extracts of strain AP-3 grown on various aromatic compounds; Indication that constitutive synthesis of enzymes is involved in 2-aminophenol metabolism, while inducible synthesis of enzymes is involved in catechol and protocatechuate metabolism in the strain.