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The structure of alanine racemase from Bacillus stearothermophilus (Geobacillus stearothermophilus) was determined by X-ray crystallography to a resolution of 1.9 A. [7] The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of beta-strand. A ...
Human epimerases include methylmalonyl-CoA epimerase, involved in the metabolic breakdown of the amino acids alanine, isoleucine, methionine and valine, [2] and UDP-glucose 4-epimerase, which is used in the final step of galactose metabolism - catalyzing the reversible conversion of UDP-galactose to UDP-glucose.
This list contains a list of EC numbers for the fifth group, EC 5, isomerases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
alanine racemase, methionine racemase: EC 5.1.2: Acting on Hydroxy Acids and Derivatives: lactate racemase, tartrate epimerase: EC 5.1.3: Acting on Carbohydrates and Derivatives: ribulose-phosphate 3-epimerase, UDP-glucose 4-epimerase: EC 5.1.99: Acting on Other Compounds: methylmalonyl CoA epimerase, hydantoin racemase
[10] [11] As a cyclic analogue of D-alanine, cycloserine acts against two crucial enzymes important in the cytosolic stages of peptidoglycan synthesis: alanine racemase (Alr) and D-alanine:D-alanine ligase (Ddl). [11] The first enzyme is a pyridoxal 5'-phosphate-dependent enzyme which converts the L-alanine to the D-alanine form. [11]
In this example, alanine is depicted in the zwitterionic form at physiological pH. D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins.
L-Alanine is produced industrially by decarboxylation of L-aspartate by the action of aspartate 4-decarboxylase. Fermentation routes to L-alanine are complicated by alanine racemase. [14] Racemic alanine can be prepared by the condensation of acetaldehyde with ammonium chloride in the presence of sodium cyanide by the Strecker reaction, [15]
DAPDC is a PLP-dependent enzyme belonging to the alanine racemase family. [4] This enzyme is generally dimeric with each monomer containing two domains. [5] The first domain is the N-terminal α/β-barrel that binds the PLP to the active site lysine residue. [3] [4] [5] The second domain is the C-terminal β-sandwich.