Bacillus d-stereospecific metallo-amidohydrolase: Active-site metal-ion substitution changes substrate specificity

Biochimie

Volumn 91, Issue 4, 2009, Pages 568-576

  Arima, Jiro ^a   Uesugi, Yoshiko ^b   Hatanaka, Tadashi ^b  

^a TOTTORI UNIVERSITY   (Japan)

^b Research Institute for Biological Science OKAYAMA   (Japan)

Author keywords

Bacillus; d aminoacyl derivatives; d stereospecific amidohydrolase; Metal substitution; Substrate specificity

Indexed keywords

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACILLUS; CATALYTIC DOMAIN; CATIONS, DIVALENT; HYDROLYSIS; METALS; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

BACILLUS SP.; BACILLUS SUBTILIS; LACTOBACILLUS FERMENTUM;

EID: 62649175724     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.01.015     Document Type: Article

References (36)

1. Walsh C.T. Enzymes in the d-Alanine branch of bacterial cell wall peptidoglycan assembly. J. Biol. Chem 264 (1989) 2393-2396
2. Casado F.J., Sánchez A.H., Rejano L., and Montaño A. d-Amino acid formation in sterilized alkali-treated olives, J. Agric. Food Chem 55 (2007) 3503-3507
3. Ogawa T., Fukuda M., and Sasaoka K. Occurrence of N-malonyl-d-alanine in pea seedlings. Biochim. Biophys. Acta 297 (1973) 60-69
4. Yokoyama T., Kan-no N., Ogata T., Kotaki Y., Sato M., and Nagahisa E. Presence of free d-amino acids in microalgae. Biosci. Biotechnol. Biochem 67 (2003) 388-392
5. Hashimoto A., Nishikawa T., Oka T., and Takahashi K. Endogenous d-serine in rat brain: N-methyl-d-aspartate receptor-related distribution and aging. J. Neurochem 60 (1993) 738-786
6. Hashimoto A., and Oka T. Free d-aspartate and d-serine in the mammalian brain and periphery, Prog. Neurobiol (1997) 325-353
7. Sarower M.G., Matsui T., and Abe H. Distribution and characteristics of d-amino acid and d-aspartate oxidases in fish tissues, J. Exp. Zoolog. A. Comp. Exp. Biol 295 (2003) 151-159
8. D'Aniello A., Di Fiore M.M., Fisher G.H., Milone A., Seleni A., D'Aniello S., Perna A.F., and Ingrosso D. Occurrence of d-aspartic acid and N-methyl-d-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release. FASEB J 14 (2000) 699-714
9. Mothet J.P., Parent A.T., Wolosker H., Brady Jr. R.O., Linden D.J., Ferris C.D., Rogawski M.A., and Snyder S.H. d-Serine is an endogenous ligand for the glycine site of the N-methyl-d-aspartate receptor. Proc. Natl. Acad. Sci. USA 97 (2000) 4926-4931
10. Wolosker H., D'Aniello A., and Snyder S.H. d-Aspartate disposition in neuronal and endocrine tissues: ontogeny, biosynthesis and release. Neuroscience 100 (2000) 183-189
11. Asano Y., and Lübbehüsen T.L. Enzymes acting on peptides containing d-amino-acid. J. Biosci. Bioeng 89 (2000) 295-306
12. Schulze Y.B., and Wubbolts M.G. Biocatalysis for industrial production of fine chemicals. Curr. Opin. Biotech 10 (1999) 609-615
13. Wakayama M., Yoshimune K., Hirose Y., and Moriguchi M. Production of d-amino acids by N-acyl-d-amino acid amidohydrolase and its structure and function. J. Mol. Catal. B Enzym 23 (2003) 71-85
14. Höltje J.V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62 (1998) 181-203
15. Arthur M., Depardieu F., Cabanié L., Reynolds P., and Courvalin P. Requirement of the VanY and VanX d,d-peptidases for glycopeptide resistance in enterococci. Mol. Microbiol. 30 (1998) 819-830
16. 2+-containing d-alanyl-d-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature 299 (1982) 469-470
17. Goffin C., and Ghuysen J.M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079-1093
18. Reynolds P.E., Depardieu F., Dutka-Malen S., Arthur M., and Courvalin P. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of d-alanyl-d-alanine. Mol. Microbiol. 13 (1994) 1065-1070
19. Asano Y., Mori T., Hanamoto S., Kato Y., and Nakazawa A. A new d-stereospecific amino acid amidase from Ochrobactrum anthropi, Biochem. Biophys. Res. Commun 162 (1989) 470-474
20. Asano Y., Nakazawa A., Kato Y., and Kondo K. Properties of a novel d-stereospecific aminopeptidase from Ochrobactrum anthropi. J. Biol. Chem. 264 (1989) 14233-14239
21. Cheggour A., Fanuel L., Duez C., Joris B., Bouillenne F., Devreese B., Van Driessche G., Van Beeumen J., Frère J.M., and Goffin C. The dppA gene of Bacillus subtilis encodes a new d-aminopeptidase. Mol. Microbiol. 38 (2000) 504-513
22. Remaut H., Bompard-Gilles C., Goffin C., Frère J.M., and Van Beeumen J. Structure of the Bacillus subtilis d-aminopeptidase DppA reveals a novel self-compartmentalizing protease. Nat. Struct. Biol. 8 (2001) 674-678
23. Asano Y., and Yamaguchi S. Dynamic kinetic resolution of amino acid amide catalyzed by d-aminopeptidase and alpha-amino-epsilon-caprolactam racemase. J. Am. Chem. Soc 127 (2005) 7696-7697
24. Yamaguchi S., Komeda H., and Asano Y. New enzymatic method of chiral amino acid synthesis by dynamic kinetic resolution of amino acid amides: use of stereoselective amino acid amidases in the presence of alpha-amino-epsilon-caprolactam racemase. Appl. Environ. Microbiol. 73 (2007) 5370-5373
25. Prescott J.M., and Wilkes S.H. Aeromonas aminopeptidase. Methods Enzymol 45 (1976) 530-543
26. Arima J., Uesugi Y., Iwabuchi M., and Hatanaka T. Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl. Microbiol. Biotechnol 70 (2006) 541-547
27. Allain C.C., Poon L.S., Chan C.S., Richmond W., and Fu P.C. Enzymatic determination of total serum cholesterol. Clin. Chem. 20 (1974) 470-475
28. D'Aniello A., Vetere A., and Petrucelli L. Further study on the specificity of d-amino acid oxidase and d-aspartate oxidase and time course for complete oxidation of d-amino acids. Comp. Biochem. Physiol. B. 105 (1993) 731-734
29. Neims A.H., De Luca D.C., and Hellerman L. Studies on crystalline d-amino acid oxidase. 3. Substrate specificity and sigma-rho relationship. Biochemistry 5 (1966) 203-212
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
31. Ben-Meir D., Spungin A., Ashkenazi R., and Blumberg S. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur. J. Biochem 212 (1993) 107-112
32. Cappiello M., Lazzaretti A., Buono F., Scaloni A., D'Ambrosio C., Amodeo P., Mendez B.L., Pelosi P., Del Corso A., and Mura U. New role for leucyl aminopeptidase in glutathione turnover. Biochem. J. 378 (2004) 35-44
33. Cappiello M., Alterio V., Amodeo P., Del Corso A., Scaloni A., Pedone C., Moschini R., De Donatis G.M., De Simone G., and Mura U. Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase. Biochemistry 45 (2006) 3226-3234
34. Holland D.R., Hausrath A.C., Juers D., and Matthews B.W. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci. 4 (1995) 1955-1965
35. Kishishita S., Okajima T., Kim M., Yamaguchi H., Hirota S., Suzuki S., Kuroda S., Tanizawa K., and Mure M. Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes. J. Am. Chem. Soc 125 (2003) 1041-1055
36. Li J.Y., Chen L.L., Cui Y.M., Li J., Nan F.J., and Ye Q.Z. Specificity for inhibitors of metal-substituted methionine aminopeptidase. Biochem. Biophys. Res. Commun 37 (2003) 172-179