A8936
Alanine Racemase from Bacillus stearothermophilus
lyophilized powder, ≥10 IU/mg solid
form
lyophilized powder
specific activity
≥10 IU/mg solid
mol wt
Mr 78 kDa (2 subunits 39 kDa each)
storage temp.
−20°C
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Application
Alanine racemase is used to convert L-alanine into D-alanine. Alanine racemase, from Sigma, has been used to isomerize L-[U-14C]alanine to a racemic mixture of L/D- [14C]alanine .
Biochem/physiol Actions
Alanine racemase is involved in alanine, aspartate and D-alanine metabolism. 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit alanine racemase. Alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N-terminus and a C-terminal domain. The N-terminus includes residues 1-240, whereas the C-terminal comprises of the β-strand (residues 241-388). One molecule of pyridoxalphosphate (PLP) is present as the cofactor in each subunit.
Physical form
Lyophilized from 50 mM phosphate buffer, pH 7.5
Other Notes
One unit will convert 1.0 μmole of D-alanine to L-alanine per minute at pH 10.5 at 30 °C in a coupled assay system with L-alanine dehydrogenase.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Yen-Lin Lin et al.
Biochimica et biophysica acta, 1814(11), 1438-1446 (2011-05-24)
Molecular dynamics simulations using a combined quantum mechanical and molecular mechanical (QM/MM) potential have been carried out to investigate the internal proton transfer equilibrium of the external aldimine species in l-dopa decarboxylase, and carbanion stabilization by the enzyme cofactor in
Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases.
Jiansong Ju et al.
Journal of biochemistry, 149(1), 83-89 (2010-10-26)
From the reaction mechanism and crystal structure analysis, a bacterial alanine racemase is believed to work as a homodimer with a substrate, l-alanine or d-alanine. We analysed oligomerization states of seven alanine racemases, biosynthetic and catabolic, from Escherichia coli, Salmonella
J P Shaw et al.
Biochemistry, 36(6), 1329-1342 (1997-02-11)
The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N-terminus, which includes residues 1-240
Naoko Yoshikawa et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 879(29), 3283-3288 (2011-05-20)
The distribution of D-amino acids was examined on several tissues of kuruma prawn Marsupenaeus japonicus. D-Alanine was found in all tissues, and the ratio of D-alanine to total alanine ranged from 18.7 to 43.7% depending on the tissues. Of these
Tien-Thanh Nguyen et al.
Journal of agricultural and food chemistry, 59(10), 5617-5624 (2011-04-21)
Food-grade gene expression systems for lactic acid bacteria are useful for applications in the food industry. We describe a new food-grade host/vector system for Lactobacillus plantarum based on pSIP expression vectors and the use of the homologous alanine racemase gene
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