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Publikováno v:
Journal of Biological Chemistry. 292:12296-12310
o-Succinylbenzoyl-CoA (OSB-CoA) synthetase (MenE) is an essential enzyme in bacterial vitamin K biosynthesis and an important target in the development of new antibiotics. It is a member of the adenylating enzymes (ANL) family, which reconfigure thei
Publikováno v:
Journal of Biological Chemistry. 292:10321-10327
Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles. The cage-forming enzyme lumazine synthase (LS) from Bacillus subtilis (BsLS), for examp
Autor:
S.P. Rojas-Trejo, Enrique Rudiño-Piñera, Enrique Raga-Carbajal, Clarita Olvera, Adelaida Díaz-Vilchis
Publikováno v:
The Journal of Biological Chemistry
Levansucrases (LSs) synthesize levan, a β2-6-linked fructose polymer, by successively transferring the fructosyl moiety from sucrose to a growing acceptor molecule. Elucidation of the levan polymerization mechanism is important for using LSs in the
Autor:
Sergei A. Dikanov, Robert B. Gennis, Sophia M. Yi, Kuppala V. Narasimhulu, Rimma I. Samoilova
Publikováno v:
Journal of Biological Chemistry. 285:18241-18251
Cytochrome aa(3)-600 is one of the principle respiratory oxidases from Bacillus subtilis and is a member of the heme-copper superfamily of oxygen reductases. This enzyme catalyzes the two-electron oxidation of menaquinol and the four-electron reducti
Publikováno v:
Journal of Biological Chemistry. 284:1725-1731
Bacterial RibG is a potent target for antimicrobial agents, because it catalyzes consecutive deamination and reduction steps in the riboflavin biosynthesis. In the N-terminal deaminase domain of Bacillus subtilis RibG, structure-based mutational anal
Autor:
Ken-ichi Yoshida, Masaki Kinehara, Masanori Yamaguchi, Hitoshi Ashida, Maya Ikeuchi, Tetsuro Morinaga, Yasutaro Fujita
Publikováno v:
Journal of Biological Chemistry. 283:10415-10424
The iolABCDEFGHIJ operon of Bacillus subtilis is responsible for myo-inositol catabolism involving multiple and stepwise reactions. Previous studies demonstrated that IolG and IolE are the enzymes for the first and second reactions, namely dehydrogen
Autor:
Bunzo Mikami, Akiko Kawamata, Wataru Hashimoto, Yukie Maruyama, Takafumi Itoh, Kousaku Murata, Akihito Ochiai
Publikováno v:
Journal of Biological Chemistry. 282:37134-37145
Rhamnogalacturonan (RG) lyase produced by plant pathogenic and saprophytic microbes plays an important role in degrading plant cell walls. An extracellular RG lyase YesW from saprophytic Bacillus subtilis is a member of polysaccharide lyase family 11
Autor:
Shih-Tung Liu, Friedrich Götz, Yu-Hsiu Lee, Ying-Chung Wu, Hung-Yu Shu, Cheng-Yeu Wu, Chyi-Liang Chen, Yu-Chieh Cheng
Publikováno v:
Journal of Biological Chemistry. 282:5608-5616
Fengycin, a lipopeptidic antibiotic, is synthesized nonribosomally by five fengycin synthetases (FenC, FenD, FenE, FenA, and FenB) in Bacillus subtilis F29-3. This work demonstrates that these fengycin synthetases interlock to form a chain, which coi
Publikováno v:
Journal of Biological Chemistry. 280:39601-39608
Arsenate reductase encoded by the chromosomal arsC gene in Bacillus subtilis catalyzes the intracellular reduction of arsenate to arsenite, which is then extruded from cells through an efficient and specific transport system. Herein, we present the s
Publikováno v:
Journal of Biological Chemistry. 280:9192-9202
The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed, purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein endowed with an unusually high oxygen affinity (in the nanomolar range) such tha