Alanine racemase
From Proteopedia
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| - | <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 == | == 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. | + | '''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 == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | AR uses 2 catalytic bases for the reaction: Lys and Tyr. | + | 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 == | == 3D Structures of alanine racemase == | ||
| + | [[Alanine racemase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | + | == References == | |
| - | + | <references/> | |
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[[Category: Topic Page]] | [[Category: Topic Page]] | ||
Current revision
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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
