Alanine racemase
From Proteopedia
(Difference between revisions)
(21 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | <StructureSection load='1l6g' size='350' side='right' caption='Structure of alanine racemase dimer complex with phosphopyridoxyl-alanine (PDB entry [[1l6g]])' scene=''> | + | <StructureSection load='1l6g' size='350' side='right' caption='Structure of alanine racemase dimer complex with phosphopyridoxyl-alanine (in magenta) (PDB entry [[1l6g]])' scene='55/551209/Cv/1'> |
- | + | == Function == | |
- | + | '''Alanine racemase''' (AR) catalyzes the racemization of L-alanine to D-alanine. AR uses pyridoxal-5’-phosphate (PLP) as a cofactor. PLP binds to a lysine residue of AR. AR participates in alanine and aspartate metabolism. <ref name="Ad">PMID:11886871</ref> | |
- | + | == Disease == | |
- | + | The antibiotic D-cycloserine is an effective inhibitor of AR. | |
- | == | + | == Relevance == |
- | + | The D-alanine produced by AR is used for peptidoglycan biosynthesis. Peptidoglycans are found in cell walls of bacteria hence AR inhibitors are tested as antimicrobial drugs. | |
- | + | ||
- | + | == Structural highlights == | |
- | + | ||
- | + | AR uses 2 catalytic bases for the reaction: <scene name='55/551209/Cv/3'>Lys and Tyr</scene> from different monomers.<ref name="Ad">PMID:11886871</ref> Water molecules are shown as red spheres. <scene name='55/551209/Cv/5'>Whole active site</scene>. | |
- | + | ||
- | + | == 3D Structures of alanine racemase == | |
- | + | [[Alanine racemase 3D structures]] | |
- | + | ||
- | + | ||
- | [[ | + | |
- | + | </StructureSection> | |
- | + | == References == | |
- | + | <references/> | |
- | [[ | + | [[Category: Topic Page]] |
- | + |
Current revision
|
References
- ↑ 1.0 1.1 Watanabe A, Yoshimura T, Mikami B, Hayashi H, Kagamiyama H, Esaki N. Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine. J Biol Chem. 2002 May 24;277(21):19166-72. Epub 2002 Mar 8. PMID:11886871 doi:10.1074/jbc.M201615200