Characterization of Psychrophilic Alanine Racemase fromBacillus psychrosaccharolyticus

Okubo, Yoko; Yokoigawa, Kumio; Esaki, Nobuyoshi; Soda, Kenji; Kawai, Hiroyasu

doi:10.1006/bbrc.1999.0324

Cited by 43 publications

(28 citation statements)

References 32 publications

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“…The catalytic activities, in the direction from the L-to D-alanine, of the homodimeric alanine racemases from B. stearothermophilus (2550 units/mg at 37°C) (11), B. psychrosaccharolyticus (2000 units/mg at 30°C) (17), and P. fluorescens (2400 units/mg at 30°C) (15) are higher than those of the monomeric alanine racemases from Shigella alr (210 units/mg at 30°C) (this paper), Sa. typhimurium alr (36 units/mg at 30°C) (12) and T. thermophilus (D-to L-alanine direction, 220 units/mg at 25°C) (14).…”

Section: Discussionmentioning

confidence: 99%

“…These differences may reflect their structural difference. We previously reported that distinguishing hydrophilic amino acid residues in the B. psychrosaccharolyticus alr enzyme interacted with solvent and reduced the compactness of the molecule leading to the low affinity for PLP (17). Then, we compared the hydropathy profile of the S. dysenteriae alr enzyme with that of the Sa.…”

Section: Discussionmentioning

confidence: 99%

“…Several kinds of alanine racemases from bacteria were purified and characterized (11)(12)(13)(14). We also reported the structure and function of psychrophilic alanine racemases from Pseudomonas fluorescens and Bacillus psychrosaccharolyticus (15)(16)(17)(18)(19)(20). A few alanine racemases from opportunistic bacterial pathogens (Pseudomonas aeruginosa and Mycobacterium avium) were recently purified and analyzed in some properties (21,22).…”

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confidence: 99%

“…The monomeric enzymes are those from Salmonella typhimurium (12,13), Thermus thermophilus (14), Schizosaccharomyces pombe (3), and a crayfish Procambarus clarkii (4). The homodimeric enzymes are those from B. stearothermophilus (11), B. psychrosaccharolyticus (17), and P. fluorescens (15). The trimeric or tetrameric enzymes are those from a brackish-water mollusc Corbicula japonica (5) and a fungus Tolypocladium niveum (1).…”

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confidence: 99%

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Gene Cloning and Characterization of Alanine Racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei

Yokoigawa

Hirasawa

Ueno

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Gene Cloning and Characterization of Alanine Racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei

Yokoigawa

Hirasawa

Ueno

et al. 2001

Biochemical and Biophysical Research Communications

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“…Bacterial alanine racemases are classified as monomeric (13,15,18) or homodimeric (3,11,12) based on the structure of their subunits. SDS-PAGE revealed that the molecular mass of the purified rAlr of B. anthracis was≈45 kDa.…”

Section: Determination Of the Molecular Mass Of Ralrmentioning

confidence: 99%

Biochemical characterization of Alanine racemase- a spore protein produced by Bacillus anthracis

Kanodia¹,

Agarwal²,

Singh³

et al. 2009

BMB Reports

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Alanine racemase catalyzes the interconversion of L-alanine and D-alanine and plays a crucial role in spore germination and cell wall biosynthesis. In this study, alanine racemase produced by Bacillus anthracis was expressed and purified as a monomer in Escherichia coli and the importance of lysine 41 in the cofactor binding octapeptide and tyrosine 270 in catalysis was evaluated. The native enzyme exhibited an apparent Km of 3 mM for L-alanine, and a Vmax of 295 μmoles/min/mg, with the optimum activity occurring at 37 o C and a pH of 8-9. The activity observed in the absence of exogenous pyridoxal 5 -phosphate suggested that the cofactor is bound to the enzyme. Additionally, the UV-visible absorption spectra indicated that the activity was pH independece, of VV-visible absorption spectra suggests that the bound PLP exists as a protonated Schiff's base. Furthermore, the loss of activity observed in the apoenzyme suggested that bound PLP is required for catalysis. Finally, the enzyme followed non-competitive and mixed inhibition kinetics for hydroxylamine and propionate with a Ki of 160 μM and 30 mM, respectively. [BMB reports 2009; 42(1): 47-52]

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Isomerazation

Esaki¹,

Kurihara²,

Soda³

2002

Enzyme Catalysis in Organic Synthesis

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Characterization of Psychrophilic Alanine Racemase fromBacillus psychrosaccharolyticus

Cited by 43 publications

References 32 publications

Gene Cloning and Characterization of Alanine Racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei

Gene Cloning and Characterization of Alanine Racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei

Biochemical characterization of Alanine racemase- a spore protein produced by Bacillus anthracis

Isomerazation

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