Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli

Journal of Basic Microbiology

Volumn 51, Issue 2, 2011, Pages 129-135

  Baek, Jin Oh ^a,b   Seo, Jeong Woo ^a   Kwon, Ohsuk ^a   Seong, Su Il ^c   Kim, Ik Hwan ^b   Kim, Chul Ho ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Korea University   (South Korea)

^c AmorePacific Corporation   (South Korea)

Author keywords

Amino acid deaminase; Ferric chloride; Phenyllactic acid; Phenylpyruvic acid; Proteus mirabilis

Indexed keywords

AMMONIA LYASE; BACTERIAL DNA; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PROTEUS MIRABILIS; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; AMMONIA-LYASES; BASE SEQUENCE; CLONING, MOLECULAR; DNA, BACTERIAL; ESCHERICHIA COLI; KINETICS; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROTEUS MIRABILIS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; PROTEUS MIRABILIS; PROTEUS VULGARIS;

EID: 79954545667     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.201000086     Document Type: Article

References (31)

1. Moustafa, I.M., Foster, S., Lyubimov, A.Y., Vrielink, A., 2006. Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism. J. Mol. Biol., 364, 991-1002.
2. Faust, A., Niefind, K., Hummel, W., Schomburg, D., 2007. The structure of a bacterial L-amino acid oxidase from Rhococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J. Mol. Biol., 367, 234-248.
3. Du, X.Y., Clemetson, K.J., 2002. Snake venom L-amino acid oxidases. Toxicon., 40, 659-665.
4. Drechsel, H., Thieken, A., Reissbrodt, R., Jung, G., Winkelmann, G., 1993. α-Keto acids are novel siderophores in the genera Proteus, Providencia, and Morganella and are produced by amino acid deaminases. J. Bacteriol., 175, 2727-2733.
5. Evanylo, L.P., Kadis, S., Maudsley, J.R., 1984. Siderophore production in Proteus mirabilis. Can. J. Microbiol., 30, 1046-1051.
6. Rubin, R.H., Tolkoff-Rubin, N.E., Cotran, R.S., 1986. Urinary tract infrction, pyelonephritis, and reflux nephropathy. In: Brenner, B.M., Rector, R.C. Jr. (eds.), The Kidney (3rd ed.), Vol. 2. Philadelphia: The W. B. Saunders Co. pp. 1085-1141.
7. Setia, U., Serventi, I., Lorenz, P., 1984. Bacteremia in a long-term care facility: spectrum and mortality. Arch. Intern. Med., 144, 1633-1635.
8. Baek, J.O., Seo, J.W., Kwon, O., Seong, S.I., Kim, I.H., Kim, C.H., 2008. Heterologous expression and characterization of L-amino acid deaminase from Proteus mirabilis in Escherichia coli. Chi. J. Biotechnol., 24, 2129.
9. Lavermicocca, P., Valerio, F., Evidente, A., Lazzaroni, S., Corsetti, A., Gobbetti, M., 2000. Purification and characterization of novel antifungal compounds from the sourdough Lactobacillus plantarum strain 21B. Appl. Environ. Microbiol., 66, 4084-4090.
10. Lavermicocca, P., Valerio, F., Visconti, A., 2003. Antifungal activity of phenyllactic acid against molds isolated from bakery products. Appl. Environ. Microbiol., 69, 634-640.
11. Ström, K., Sjögren, J., Broberg, A., Schnürer, J., 2002. Lactobacillus plantarum MiLAB 393 produces the antifungal cyclic dipeptides cyclo(L-Phe-L-Pro) and cyclo(L-Phe-trans -4-OH-L-Pro) and 3-phenyllactic acid. Appl. Environ. Microbiol., 68, 4322-4327.
12. Valerio, F., Lavermicocca, P., Pascale, M., Visconti, A., 2004. Production of phenyllactic acid by lactic acid bacteria: an approach to the selection of strains contributing to food quality and preservation. FEMS. Microbiol. Lett., 233, 289-295.
13. Takahashi, E., Furui, M., Seko, H., Shibatani, T., 1997. D-Methionine preparation from racemic methionines by Proteus vulgaris IAM 12002 with asymmetric degrading activity. Appl. Microbiol. Biotechnol., 47, 173-179.
14. Beers, R.F., Jr., Sizer, I.W., 1952. A spectrophotometric method for measuring the breakdown of oxygen peroxide by catalase. J. Biol. Chem., 195, 133-140.
15. Pelmont, J., Arlaud, G., Rossat, A.M., 1972. L-aminoacid oxydases des envelopes de Proteus mirabilis: proprietes generales. Biochimie., 54, 1359-1374.
16. Duerre, J., Chakrabarty, S., 1975. L-amino acid oxidase of Proteus rettgeri. J. Bacteriol., 121, 656-663.
17. Sambrook, J., Fritsch, E.F., Maniatis, T., 1989. Molecular Cloning: a Laboratory Manual (2nd ed.). New York: Cold Spring Harbor Laboratory, Cold Spring Harbor.
18. Pearson, M.M., Sebaihia, M., Churcher, C., Quail, M.A., et al., 2008. Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility. J. Bacteriol., 190, 4027-4037.
19. Massad, G., Zhao, H., Mobley, H.L.T., 1995. Proteus mirabilis amino acid deaminase: cloning, nucleotide, sequence, and characterization of aad. J. Bacteriol., 177, 5878-5883.
20. Takahashi, E., Ito, K., Yochimoto, T., 1999. Cloning of L-amino acid deaminase gene from Proteus vulgaris. Biosci. Biotechnol. Biochem., 63, 2244-2247.
21. Dym, O., Eisenberg, D., 2001. Sequence-structure analysis of FAD-containing proteins. Protein Scie., 10, 1712-1728.
22. Vallon, O., 2000. Sequence motifs in flavoproteins: evidence for common ancestry and tools to predict structure. Proteins: Struct. Funct. Genets., 38, 95-114.
23. Geueke, B., Hummel, W., 2002. A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization. Enzyme. Microb. Technol., 31, 77-87.
24. Geueke, B., Hummel, W., 2003. Heterologous expression of Rhodococcus opacus L-amino acid oxidase in Streptomyces lividans. Protein. Express. Purif., 28, 303-309.
25. Pantaleone, D.P., Geller, A.M., Taylor, P.P., 2001. Purification and characterization of an L-amino acid deaminase used to prepare unnatural amino acids. J. Mol. Catal., 11, 795-803.
26. Fernandez, M., Zuniga, M., 2006. Amino acid catabolic pathways of lactic acid bacteria. Crit. Rev. Microbiol., 32, 155-183.
27. Kolenbrander, H. M., Berg, C. P., 1967. Role of urocanic acid in the metabolism of L-histidine. Arch. Biochem. Biophys., 119, 110-118.
28. Zannoni, V. G., La Du, B. N., 1963. Determination of histidine alpha-deaminase in human stratum corneum and its absence in histidinaemia. Biochem. J., 88, 160-162.
29. Nissim, I., 1999. Newer aspects of glutamine/glutamate metabolism: the role of acute pH changes. Am. J. Physiol., 277, F493-F497.
30. Bogusky, R.T., Lowenstein, L.M., Aoki, T.T., 1983. The relationship between glutamate deamination and gluconeogenesis in kidney. Biochem. J., 210, 695-698.
31. Al-Awadi, F.M., 1982. Activity of adenylate deaminase and glutamate dehydrogenase in the liver: species and dietary variation. Comp. Biochem. Physiol. B., 71, 605-609.