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
Looking for similar products? Visit Product Comparison Guide
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Seung Hyuk Choi et al.
Fish & shellfish immunology, 31(1), 58-65 (2011-03-15)
Two auxotrophic genes that play essential roles in bacterial cell wall biosynthesis--alanine racemase (alr) gene and aspartate semialdehyde dehydrogenase (asd) gene--knock-out Edwardsiella tarda (Δalr Δasd E. tarda) was generated by the allelic exchange method to develop a combined vaccine system.
Amir Rubinstein et al.
Biochemistry, 49(18), 3957-3964 (2010-04-17)
Alanine racemase (AlaR) catalyzes the interconversion between l-Ala and d-Ala with the aid of the cofactor pyridoxal 5'-phosphate (PLP). The pyridine nitrogen in PLP in the wild-type enzyme is unprotonated due to interaction with Arg219, a rare feature among PLP-dependent
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service