Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis

Current Opinion in Chemical Biology

Volumn 3, Issue 5, 1999, Pages 607-613

  Born, Timothy L ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIAMINOPIMELIC ACID; EPIMERASE; LYSINE; PYRIDOXAL 5 PHOSPHATE;

BACTERIAL CELL WALL; BIOSYNTHESIS; ENZYME ACTIVITY; ENZYME CONFORMATION; REVIEW;

BACTERIA (MICROORGANISMS);

EID: 0032831101     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00016-2     Document Type: Review

References (22)

1. Work E A new naturally occurring amino acid. Nature. 165:1950;74-75.
2. Gilvarg C Biosynthesis of diaminopimelic acid. Feder Proc. 19:1960;948-952.
3. Scapin G, Blanchard JS Enzymology of bacterial lysine biosynthesis. Adv Enzymol. 72:1998;279-324. This review describes work prior to this review, on all of the enzymes involved in the DAP/lysine biosynthetic pathway, in much greater detail.
4. Bairoch A The PROSITE dictionary of sites and patterns in proteins, and its current status. Nucleic Acids Res. 13:1993;3097-3103.
5. Beamon T, Blanchard JS, Roderick SL The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase. Biochemistry. 37:1998;10363-10369. This paper describes crystal structures of tetrahydrodipicolinate N-succinyltransferase with bound substrates, identifying the substrate binding sites and geometry of binding.
6. Berges DA, DeWolf WE, Dunn GL, Newman DJ, Schmidt SJ, Taggart JJ, Gilvarg C Studies on the active site of succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. J Biol Chem. 261:1986;6160-6167.
7. Cox RJ, Sherwin WA, Lam LKP, Vederas JC Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-L,L-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli. J Am Chem Soc. 118:1996;7449-7460.
8. Ledwidge R, Blanchard JS The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis. Biochemistry. 38:1999;3019-3024. A description of the ability of NAcOATase to catalyze both its namesake reaction and the corresponding reaction in lysine biosynthesis. It provides a possible explanation for the inability to clone DapATase.
9. Lin Y, Myhrman R, Schrag ML, Gelb MH Bacterial N-succinyl-L-diaminopimelic acid desuccinylase. J Biol Chem. 263:1988;1622-1627.
10. 2, a bacterial enzyme with applications in cancer therapy. Structure. 5:1997;337-347.
11. Born TL, Zheng R, Blanchard JS Hydrolysis of N-succinyl-L,L-diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: metal activation, solvent isotope effects, and kinetic mechanism. Biochemistry. 37:1998;10478-10487. A detailed kinetic description of the desuccinylase that describes similarities to the family of metal dependent amidases such as metallo-β-lactamases and matrix metalloproteinases.
12. 2+-substituted carbonic anhydrase II. J Biol Chem. 262:1987;16417-16424.
13. Tanner ME, Gallo KA, Knowles JR Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase. Biochemistry. 32:1993;3998-4006.
14. Cardinale GJ, Abeles RH Purification and mechanism of action of proline racemase. Biochemistry. 7:1968;3970-3978.
15. Cirilli M, Zheng R, Scapin G, Blanchard JS Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 37:1998;16452-16458. Presents the first crystal structure of a member of the family of PLP-independent amino acid racemases, which currently has no structural homologue.
16. Hwang KY, Cho C-S, Kim SS, Sung H-C, Yu YG, Cho Y Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat Struct Biol. 6:1999;422-426.
17. Higgins W, Tardif C, Richaud C, Krivanek MA, Cardin A Expression of recombinant diaminopimelate epimerase in Escherichia coli. Eur J Biochem. 186:1989;137-143.
18. 2O.
19. Misono H, Soda K Properties of meso-α,ε-diaminopimelate D-dehydrogenase from Bacillus sphaericus. J Biol Chem. 255:1980;10599-10605.
20. Scapin G, Reddy SG, Blanchard JS Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. Biochemistry. 35:1996;13540-13551.
21. Scapin G, Cirilli M, Reddy SG, Gao Y, Vederas JC, Blanchard JS Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase. Biochemistry. 37:1998;3278-3285. Describes the crystal structure of DapDH with the substrate DAP bound at the active site. Also describes the binding of a competitive inhibitor that explains its mechanism of inhibition.
22. Sutherland A, Caplan JF, Vederas JC Unsaturated α-aminopimelic acids as potent inhibitors of meso-diaminopimelic acid (DAP) D-dehydrogenase. Chem Commun. 1999;555-556.