Enzyme

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EC Tree
     5. Isomerases
        5.1 Racemases and epimerases
            5.1.2 Acting on hydroxy acids and derivatives
ID:5.1.2.2
Description:Mandelate racemase.
Prosite: PDOC00706;
PDB:
PDBScop
Cath: 3.20.20.120; 3.30.390.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.1.2.2
BRENDA Enzyme Link: BRENDA 5.1.2.2
KEGG Enzyme Link: KEGG5.1.2.2
BioCyc Enzyme Link: BioCyc 5.1.2.2
ExPASy Enzyme Link: ExPASy5.1.2.2
EC2PDB Enzyme Link: EC2PDB 5.1.2.2
ExplorEnz Enzyme Link: ExplorEnz 5.1.2.2
PRIAM enzyme-specific profiles Link: PRIAM 5.1.2.2
IntEnz Enzyme Link: IntEnz 5.1.2.2
MEDLINE Enzyme Link: MEDLINE 5.1.2.2
MSA:

5.1.2.2;

Phylogenetic Tree:

5.1.2.2;

Uniprot:
M-CSA:
RHEA:13945 (S)-mandelate = (R)-mandelate
RULE(radius=1)
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL1996 May 78639525
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL1995 Mar 77893690
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL1995 Mar 77893689
Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant.Landro JA, Kallarakal AT, Ransom SC, Gerlt JA, Kozarich JW, Neidhart DJ, Kenyon GL1991 Sep 241909893
The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes.GUNSALUS CF, STANIER RY, GUNSALUS IC1953 Nov13108854