DapE can function as an aspartyl peptidase in the presence of Mn2+

Journal of Bacteriology

Volumn 185, Issue 16, 2003, Pages 4748-4754

  Broder, Daniel H ^a   Miller, Charles G ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; ASPARTIC PROTEINASE; ASPARTYL PEPTIDASE; GLUTAMINE; HEXAHISTIDINE; HISTIDINE DERIVATIVE; HYBRID PROTEIN; LEUCINE; MANGANESE; MANGANESE DEPENDENT PEPTIDASE; METHIONINE; N SUCCINYL DIAMINOPIMELATE DESUCCINYLASE; UNCLASSIFIED DRUG; ZINC;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BACTERIAL GROWTH; BINDING AFFINITY; BINDING SITE; CATION TRANSPORT; CHROMOSOME DISORDER; CONTROLLED STUDY; DAPE GENE; ENZYME ACTIVE SITE; ENZYME PURIFICATION; EXPRESSION VECTOR; GENE CONSTRUCT; GENE DISRUPTION; GENE ISOLATION; GENE OVEREXPRESSION; HYDROLYSIS; METAL BINDING; MOLECULAR CLONING; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PURIFICATION; SALMONELLA ENTERICA; SALMONELLA TYPHIMURIUM; STRAIN DIFFERENCE; STRAIN IDENTIFICATION;

AMIDOHYDROLASES; ASPARTIC ENDOPEPTIDASES; BINDING SITES; KINETICS; MANGANESE; MUTATION; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; SUBSTRATE SPECIFICITY; ZINC;

ANIMALIA; BACTERIA (MICROORGANISMS); NEGIBACTERIA; SALMONELLA ENTERICA; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM; SALMONELLA TYPHIMURIUM; VECTORS;

EID: 0041559790     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.16.4748-4754.2003     Document Type: Article

References (33)

1. Abbott, J. J., J. Pei, J. L. Ford, Y. Qi, V. N. Grishin, L. A. Pitcher, M. A. Phillips, and N. V. Grishin. 2001. Structure prediction and active site analysis of the metal binding determinants in gamma-glutamylcysteine synthetase. J. Biol. Chem. 276:42099-42107.
2. Archibald, F. S., and I. Fridovich. 1982. The scavenging of superoxide radical by manganous complexes: in vitro. Arch. Biochem. Biophys. 214:452-463.
3. Barrett, A. J., N. D. Rawlings, and J. F. Woessner. 1998. Handbook of proteolytic enzymes. Academic Press, San Diego, Calif.
4. Berlett, B. S., P. B. Chock, B. B. Yim, and E. R. Stadtman. 1990. Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide. Proc. Natl. Acad. Sci. USA 87:389-393.
5. Born, T. L., R. Zheng, and J. S. Blanchard. 1998. Hydrolysis of N-succinyl-L, L-diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: metal activation, solvent isotope effects, and kinetic mechanism. Biochemistry 37:10478-10487.
6. Boyen, A., D. Charlier, J. Charlier, V. Sakanyan, I. Mett, and N. Glansdorff. 1992. Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related. Gene 116:1-6.
7. 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content. J. Biol. Chem. 248:294-304.
8. Carter, T. H., and C. G. Miller. 1984. Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E. J. Bacteriol. 159:453-459.
9. Chen, G., T. Edwards, V. M. D'Souza, and R. C. Holz. 1997. Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: a two-metal ion mechanism for peptide hydrolysis. Biochemistry 36:4278-4286.
10. Conlin, C. A., K. Håkensson, A. Liljas, and C. G. Miller. 1994. Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an a-aspartyl dipeptidase. J. Bacteriol. 176:166-172.
11. Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
12. Gary, J. D., and S. Clarke. 1995. Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli. J. Biol. Chem. 270:4076-4087.
13. Håkansson, K., and C. G. Miller. 2002. Structure of peptidase T from Salmonella typhimurium. Eur. J. Biochem. 269:443-450.
14. Håkansson, K., A. H. Wang, and C. G. Miller. 2000. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc. Natl. Acad. Sci. USA 97:14097-14102.
15. Javid-Majd, F., and J. S. Blanchard. 2000. Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase. Biochemistry 39:1285-1293.
16. 2+ transporter of Salmonella enterica serovar Typhimurium. J. Bacteriol. 184:3159-3166.
17. Kim, H., and W. N. Lipscomb. 1993. Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography. Proc. Natl. Acad. Sci. USA 90:5006-5010.
18. 2+ ions during formation of Mn-bicarbonate complexes. Membr. Cell Biol. 11:115-120.
19. Larsen, R. A., T. M. Knox, and C. G. Miller. 2001. Aspartic peptide hydrolases in Salmonella enterica serovar Typhimurium. J. Bacteriol. 183:3089-3097.
20. Lassy, R. A. L., and C. G. Miller. 2000. Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182:2536-2543.
21. Lin, Y. K., R. Myhrman, M. L. Schrag, and M. H. Gelb. 1988. Bacterial N-succinyl-L-diaminopimelic acid desuccinylase. Purification, partial characterization, and substrate specificity. J. Biol. Chem. 263:1622-1627.
22. Makarova, K. S., and N. V. Grishin. 1999. The Zn-peptidase superfamily: functional convergence after evolutionary divergence. J. Mol. Biol. 292:11-17.
23. Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
24. Mathew, Z., T. M. Knox, and C. G. Miller. 2000. Salmonella enterica serovar Typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids. J. Bacteriol. 182:3383-3393.
25. Miller, C. G. 1996. Protein degradation and proteolytic modification, p. 938-954. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
26. Miller, C. G., A. M. Kukral, J. L. Miller, and N. R. Movva. 1989. pepM is an essential gene in Salmonella typhimurium. J. Bacteriol. 171:5215-5217.
27. Miller, C. G., and K. Mackinnon. 1974. Peptidase mutants of Salmonella typhimurium. J. Bacteriol. 120:355-363.
28. Prescott, J., F. Wagner, B. Holmquist, and B. Vallee. 1983. One hundred fold increased activity of Aeromonas aminopeptidase by sequential substitutions with Ni(II) or Cu(II) followed by zinc. Biochem. Biophys. Res. Commun. 114:646-652.
29. Rowsell, S., R. A. Pauptit, A. D. Tucker, R. G. Melton, D. M. Blow, and P. Brick. 1997. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure 5:337-347.
30. Schmieger, H. 1972. Phage P22-mutants with increased or decreased transduction abilities. Mol. Gen. Genet. 119:75-88.
31. Sträter, N., L. Sun, E. R. Kantrowitz, and W. N. Lipscomb. 1999. A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase. Proc. Natl. Acad. Sci. USA 96:11151-11155.
32. Vogel, H. J., and D. M. Bonner. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
33. 2+ as a cofactor: a case of mistaken identity? Protein Sci. 7:2684-2687.