cd06826

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2

CDD entry
Member databaseCDD
CDD typedomain
Short namePLPDE_III_AR2
SetPLPDE_III

Description

This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
[2, 5, 4, 1, 7, 8, 6, 11, 12, 9, 3, 10]

References

1.Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product. Noda M, Matoba Y, Kumagai T, Sugiyama M. J. Biol. Chem. 279, 46153-61, (2004). View articlePMID: 15302886

2.Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes. Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F. Biochim Biophys Acta 1647, 214-9, (2003). PMID: 12686135

3.The manifold of vitamin B6 dependent enzymes. Schneider G, Kack H, Lindqvist Y. Structure 8, R1-6, (2000). View articlePMID: 10673430

4.Cluster analysis of hydration waters around the active sites of bacterial alanine racemase using a 2-ns MD simulation. Huang HC, Jupiter D, Qiu M, Briggs JM, Vanburen V. Biopolymers 89, 210-9, (2008). PMID: 18023020

5.Sequence of the putative alanine racemase operon in Staphylococcus aureus: insertional interruption of this operon reduces D-alanine substitution of lipoteichoic acid and autolysis. Kullik I, Jenni R, Berger-Bachi B. Gene 219, 9-17, (1998). PMID: 9756984

6.Role of tyrosine 265 of alanine racemase from Bacillus stearothermophilus. Watanabe A, Kurokawa Y, Yoshimura T, Esaki N. J Biochem 125, 987-90, (1999). PMID: 10348897

7.A eukaryotic alanine racemase gene involved in cyclic peptide biosynthesis. Cheng YQ, Walton JD. J Biol Chem 275, 4906-11, (2000). PMID: 10671527

8.Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine. Watanabe A, Yoshimura T, Mikami B, Esaki N. J Biochem 126, 781-6, (1999). PMID: 10502689

9.The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. Mehta PK, Christen P. Adv. Enzymol. Relat. Areas Mol. Biol. 74, 129-84, (2000). PMID: 10800595

10.Structure, evolution and action of vitamin B6-dependent enzymes. Jansonius JN. Curr. Opin. Struct. Biol. 8, 759-69, (1998). View articlePMID: 9914259

11.Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5'-phosphate. Chemical rescue studies of Lys39 --> Ala mutant. Watanabe A, Kurokawa Y, Yoshimura T, Kurihara T, Soda K, Esaki N, Watababe A. J Biol Chem 274, 4189-94, (1999). PMID: 9933615

12.From cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. Christen P, Mehta PK. Chem Rec 1, 436-47, (2001). View articlePMID: 11933250

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