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Review Article

Inhibitors of alanine racemase enzyme: a review

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Pages 517-526 | Received 02 Feb 2015, Accepted 23 Apr 2015, Published online: 29 May 2015

Figures & data

Figure 1. Pictorial view of the Bacillus stearothermophilus Alr homodimer (PBD ID: 1SFT). PLP (pyridoxyl 5′-phosphate), ACT (acetate), Lys (lysine).

Figure 1. Pictorial view of the Bacillus stearothermophilus Alr homodimer (PBD ID: 1SFT). PLP (pyridoxyl 5′-phosphate), ACT (acetate), Lys (lysine).

Figure 2. Structure of Alr inhibitor O-carbamyl-d-serine 1.

Figure 2. Structure of Alr inhibitor O-carbamyl-d-serine 1.

Figure 3. Structures of Alr inhibitor d-cycloserine 2 and l-cycloserine 3.

Figure 3. Structures of Alr inhibitor d-cycloserine 2 and l-cycloserine 3.

Figure 4. Enantiomers of β-chloroalanine as Alr inhibitor 4 and 5.

Figure 4. Enantiomers of β-chloroalanine as Alr inhibitor 4 and 5.

Figure 5. Structures of d,l-cycloserine analogs 6 as Alr inhibitors.

Figure 5. Structures of d,l-cycloserine analogs 6 as Alr inhibitors.

Figure 6. Structure of alafosfalin 7.

Figure 6. Structure of alafosfalin 7.

Figure 7. Derivatives of alafosfalin 8a–e as Alr inhibitors.

Figure 7. Derivatives of alafosfalin 8a–e as Alr inhibitors.

Figure 8. Aminomethylphosphonopeptide analogs 9 as Alr inhibitors.

Figure 8. Aminomethylphosphonopeptide analogs 9 as Alr inhibitors.

Figure 9. Structures of 1-aminoethylphosphonic acid enantiomers 10a–g and 11 as Alr inhibitors.

Figure 9. Structures of 1-aminoethylphosphonic acid enantiomers 10a–g and 11 as Alr inhibitors.

Figure 10. Structures of β-d-fluoroalanine 12, β-l-fluoroalanine 13 and O-acetyl-d-serine 14 as Alr inhibitors.

Figure 10. Structures of β-d-fluoroalanine 12, β-l-fluoroalanine 13 and O-acetyl-d-serine 14 as Alr inhibitors.

Figure 11. Structures of fluorinated 1-aminoethyl phosphonic acid analogs 15–17 as Alr inhibitors.

Figure 11. Structures of fluorinated 1-aminoethyl phosphonic acid analogs 15–17 as Alr inhibitors.

Figure 12. Structures of (β-chloro-α-aminoethyl)phosphonic acid derivatives 18–20 as Alr inhibitors.

Figure 12. Structures of (β-chloro-α-aminoethyl)phosphonic acid derivatives 18–20 as Alr inhibitors.

Figure 13. Structure of dl-(1-amino-2-propeny1)phosphonic acid 21 as an Alr inhibitor.

Figure 13. Structure of dl-(1-amino-2-propeny1)phosphonic acid 21 as an Alr inhibitor.

Figure 14. Structure of 1-aminocyclopropanephosphonate 22 as an Alr inhibitor.

Figure 14. Structure of 1-aminocyclopropanephosphonate 22 as an Alr inhibitor.

Figure 15. Structure of halovinylglycines 23 as Alr inhibitors.

Figure 15. Structure of halovinylglycines 23 as Alr inhibitors.

Figure 16. Structure of l-norvalyl-l-chlorovinylglycine 24 as an Alr inhibitor.

Figure 16. Structure of l-norvalyl-l-chlorovinylglycine 24 as an Alr inhibitor.

Figure 17. Structures of peptidyl and amino acid C10-esters of deacetylcephalothin 25–29 as Alr inhibitors.

Figure 17. Structures of peptidyl and amino acid C10-esters of deacetylcephalothin 25–29 as Alr inhibitors.

Figure 18. Structure of (1-aminoethy1)boronic acid (Ala-B) 30 as an Alr inhibitor.

Figure 18. Structure of (1-aminoethy1)boronic acid (Ala-B) 30 as an Alr inhibitor.

Figure 19. Structure of Alr inhibitor β,β,β-trifluoro alanine 31.

Figure 19. Structure of Alr inhibitor β,β,β-trifluoro alanine 31.

Figure 20. Structures of non-substrate Alr inhibitors 32–39.

Figure 20. Structures of non-substrate Alr inhibitors 32–39.

Figure 21. Structure of thiadiazolidinones 40 and 41a–k as Alr inhibitors.

Figure 21. Structure of thiadiazolidinones 40 and 41a–k as Alr inhibitors.

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