| degradation of 2-ketoarginine by guanidinobutyrase in arginine aminotransferase pathway of brevibacterium helvolum. | guanidinobutyrase (ec 3.5.3.7) involved in the arginine oxygenase pathway of brevibacterium helvolum ifo 12073 was found to catalyze also the hydrolysis of 2-ketoarginine (2-keto-5-guanidinovalerate) to 2-ketoornithine (2-keto-5-aminovalerate) and urea, the second step of the arginine aminotransferase pathway. no other enzyme that degraded 2-ketoarginine was found in cells grown on l-arginine. the enzyme hydrolyzed 2-ketoarginine with a relative rate of about 0.7% of that toward 4-guanidinobutyr ... | 1995 | 7766193 |
| trehalose synthesis by sequential reactions of recombinant maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase from brevibacterium helvolum. | a dna fragment encoding two enzymes leading to trehalose biosynthesis, maltooligosyltrehalose synthase (bvmts) and maltooligosyltrehalose trehalohydrolase (bvmth), was cloned from the nonpathogenic bacterium brevibacterium helvolum. the open reading frames for the two proteins are 2,331 and 1,770 bp long, respectively, and overlap by four nucleotides. recombinant bvmts, bvmth, and fusion gene bvmtsh, constructed by insertion of an adenylate in the overlapping region, were expressed in escherichi ... | 2000 | 11055902 |
| phylogenetic studies on corynebacterium bovis isolated from bovine mammary glands. | coryneform bacteria are frequently isolated from bovine mastitis with the lipophilic species, and corynebacterium bovis is the most frequently isolated organism of this group. however, previous studies on the phylogeny of corynebacteria have incorporated only a single reference strain. we examined the phylogeny of c. bovis using 47 strains isolated from bovine mammary glands. phylogenetic studies were performed by direct sequencing of the 16s ribosomal rna and comparison to sequences of referenc ... | 2001 | 11768082 |
| screening of microbes, isolation, genetic manipulation, and physiological optimization of brevibacterium helvolum to produce and excrete thymidine and deoxyuridine in high concentrations. | analogues of deoxypyrimidines are used in the treatment of a variety of human ailments. azidothymidine, or azt, is one such analogue used to treat aids. thymidine is the precursor of azt, and its cost contributes to the high price of azt. attempts are being made to isolate and genetically manipulate microbes that can produce and excrete this compound in high concentrations. to this end, 145 different microbial species from zeneca and the american type culture collection were screened. moreover, ... | 2000 | 12483580 |
| overproduction of thymidine by recombinant brevibacterium helvolum amplified with thymidine monophosphate phosphohydrolase gene from bacteriophage pbs2. | a microbial fermentation process could be used to produce thymidine biologically but many of the enzymes related to nucleotide biosynthesis are highly regulated. to overcome the complex regulation steps, an analogue mutant of brevibacterium helvolum resistant to fluorouracil, hydroxyurea, and trimethoprim was constructed. this mutant accumulated 380 mg thymidine 1(-1) in 16 h in shake-flask culture. however, the accumulation of thymidine monophosphate (tmp) inside the cells suggested a low activ ... | 2004 | 15055759 |
| over-expression of bvmtsh, a fusion gene for maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase, enhances drought tolerance in transgenic rice. | plant abiotic stress tolerance has been modulated by engineering the trehalose synthesis pathway. however, many stress-tolerant plants that have been genetically engineered for the trehalose synthesis pathway also show abnormal development. the metabolic intermediate trehalose 6-phosphate has the potential to cause aberrations in growth. to avoid growth inhibition by trehalose 6-phosphate, we used a gene that encodes a bifunctional in-frame fusion (bvmtsh) of maltooligosyltrehalose synthase (bvm ... | 2014 | 24209631 |
| guanidinobutyrase for l-arginine degradation in brevibacterium helvolum. | guanidinobutyrase (guanidinobutyrate amidinohydrolase, ec. 3.5.3.7) catalyzing the third step of the arginine oxygenase pathway in brevibacterium helvolum ifo 12073 (atcc 11822) was purified to homogeneity and characterized. the enzyme had a molecular weight of 190,000 and was composed of four apparently identical subunits with a molecular weight of 45,000. the e(1%) value at 280 nm of the enzyme protein was 2.4. the enzyme contained 0.5 mol of firmly bound zn(2+) per mol of subunit. the enzyme ... | 1992 | 27286206 |