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Volumn 185, Issue 8, 2003, Pages 2451-2456

Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BENZALDEHYDE DEHYDROGENASE; BENZOYLFORMATE DECARBOXYLASE; GENE PRODUCT; MANDELAMIDE HYDROLASE; MANDELATE DEHYDROGENASE; MANDELATE RACEMASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN MDLD; PROTEIN MDLX; PROTEIN MDLY; UNCLASSIFIED DRUG;

EID: 0037385677     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.8.2451-2456.2003     Document Type: Article
Times cited : (26)

References (38)
  • 4
    • 0000527093 scopus 로고
    • Induction and repression of Pseudomonas aeruginosa amidase
    • Brammar, W. J., and P. H. Clarke. 1964. Induction and repression of Pseudomonas aeruginosa amidase. J. Gen. Microbiol. 37:307-319.
    • (1964) J. Gen. Microbiol. , vol.37 , pp. 307-319
    • Brammar, W.J.1    Clarke, P.H.2
  • 5
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner, S. 1988. The molecular evolution of genes and proteins: a tale of two serines. Nature 334:528-530.
    • (1988) Nature , vol.334 , pp. 528-530
    • Brenner, S.1
  • 7
    • 0023890672 scopus 로고
    • Microbial metabolism of mandelate: A microcosm of diversity
    • Fewson, C. A. 1988. Microbial metabolism of mandelate: a microcosm of diversity. FEMS Microbiol. Rev. 4:85-110.
    • (1988) FEMS Microbiol. Rev. , vol.4 , pp. 85-110
    • Fewson, C.A.1
  • 8
    • 0001667709 scopus 로고
    • The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes
    • Gunsalus, C. F., R. Y. Stanier, and I. C. Gunsalus. 1953. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66:548-553.
    • (1953) J. Bacteriol. , vol.66 , pp. 548-553
    • Gunsalus, C.F.1    Stanier, R.Y.2    Gunsalus, I.C.3
  • 9
    • 0032516465 scopus 로고    scopus 로고
    • The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
    • Hasson, M. S., A. Muscate, M. J. McLeish, L. S. Polovnikova, J. A. Gerlt, G. L. Kenyon, G. A. Petsko, and D. Ringe. 1998. The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry 37:9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Muscate, A.2    McLeish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 10
    • 0013892853 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type
    • Hegeman, G. D. 1966. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type. J. Bacteriol. 91:1140-1154.
    • (1966) J. Bacteriol. , vol.91 , pp. 1140-1154
    • Hegeman, G.D.1
  • 11
    • 0034817730 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme
    • Hempel, J., I. Kuo, J. Perozich, B. C. Wang, R. Lindahl, and H. Nicholas. 2001. Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme. Eur. J. Biochem. 268:722-726.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 722-726
    • Hempel, J.1    Kuo, I.2    Perozich, J.3    Wang, B.C.4    Lindahl, R.5    Nicholas, H.6
  • 12
    • 0029996889 scopus 로고    scopus 로고
    • Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantio-selectively hydrolyzes 2-arylpropionamides
    • Hirrlinger, B., A. Stolz, and H.-J. Knackmuss. 1996. Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantio-selectively hydrolyzes 2-arylpropionamides. J. Bacteriol. 178:3501-3507.
    • (1996) J. Bacteriol. , vol.178 , pp. 3501-3507
    • Hirrlinger, B.1    Stolz, A.2    Knackmuss, H.-J.3
  • 13
    • 0014454706 scopus 로고
    • The determination of urea, ammonia, and urease
    • Kaplan, A. 1969. The determination of urea, ammonia, and urease. Methods Biochem. Anal. 17:311-324.
    • (1969) Methods Biochem. Anal. , vol.17 , pp. 311-324
    • Kaplan, A.1
  • 14
    • 0024556880 scopus 로고
    • The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase
    • Kok, M., R. Oldenhuis, M. P. van der Linden, C. H. Meulenberg, J. Kingma, and B. Witholt. 1989. The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. J. Biol. Chem. 264:5442-5451.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5442-5451
    • Kok, M.1    Oldenhuis, R.2    Van der Linden, M.P.3    Meulenberg, C.H.4    Kingma, J.5    Witholt, B.6
  • 16
    • 0034661490 scopus 로고    scopus 로고
    • Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2
    • Koo, H. M., S. O. Choi, H. M. Kim, and Y. S. Kim. 2000. Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2. Biochem. J. 349:501-507.
    • (2000) Biochem. J. , vol.349 , pp. 501-507
    • Koo, H.M.1    Choi, S.O.2    Kim, H.M.3    Kim, Y.S.4
  • 17
    • 0021918804 scopus 로고
    • An improved method of ammonia determination, applicable to amidases and other ammonia-producing enzyme systems of mycobacteria
    • Krallmann-Wenzel, U. 1985. An improved method of ammonia determination, applicable to amidases and other ammonia-producing enzyme systems of mycobacteria. Am. Rev. Respir. Dis. 131:432-434.
    • (1985) Am. Rev. Respir. Dis. , vol.131 , pp. 432-434
    • Krallmann-Wenzel, U.1
  • 18
    • 0344806548 scopus 로고
    • Selection of mandelamidase constitutive mutants in continuous culture of Pseudomonas putida
    • Laverack P. D., and P. H. Clarke. 1979. Selection of mandelamidase constitutive mutants in continuous culture of Pseudomonas putida. Biotechnol. Lett. 1:353-358.
    • (1979) Biotechnol. Lett. , vol.1 , pp. 353-358
    • Laverack, P.D.1    Clarke, P.H.2
  • 20
    • 0031921608 scopus 로고    scopus 로고
    • Cloning and characterization of the Pseudomonas aeruginosa zwf gene encoding glucose-6-phosphate dehydrogenase, an enzyme important in resistance to methyl viologen (paraquat)
    • Ma, J.-F., P. W. Hager, M. L. Howell, P. V. Phibbs, and D. J. Hassett. 1998. Cloning and characterization of the Pseudomonas aeruginosa zwf gene encoding glucose-6-phosphate dehydrogenase, an enzyme important in resistance to methyl viologen (paraquat). J. Bacteriol. 180:1741-1749.
    • (1998) J. Bacteriol. , vol.180 , pp. 1741-1749
    • Ma, J.-F.1    Hager, P.W.2    Howell, M.L.3    Phibbs, P.V.4    Hassett, D.J.5
  • 21
    • 0025604503 scopus 로고
    • Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: Structural evidence for genetic coupling with nitrile hydratase
    • Mayaux, J. F., E. Cerebelaud, F. Soubrier, D. Faucher, and D. Pétré. 1990. Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase. J. Bacteriol. 172:6764-6773.
    • (1990) J. Bacteriol. , vol.172 , pp. 6764-6773
    • Mayaux, J.F.1    Cerebelaud, E.2    Soubrier, F.3    Faucher, D.4    Pétré, D.5
  • 22
    • 0027751820 scopus 로고
    • A novel structural basis for membrane association of a protein: Construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida
    • Mitra, B., J. A. Gerlt, P. C. Babbitt, C. W. Koo, G. L. Kenyon, D. Joseph, and G. A. Petsko. 1993. A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry 32:12959-12967.
    • (1993) Biochemistry , vol.32 , pp. 12959-12967
    • Mitra, B.1    Gerlt, J.A.2    Babbitt, P.C.3    Koo, C.W.4    Kenyon, G.L.5    Joseph, D.6    Petsko, G.A.7
  • 23
    • 0025109929 scopus 로고
    • Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous
    • Neidhart, D. J., G. L. Kenyon, J. A. Gerlt, and G. A. Petsko. 1990. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature 347:692-694.
    • (1990) Nature , vol.347 , pp. 692-694
    • Neidhart, D.J.1    Kenyon, G.L.2    Gerlt, J.A.3    Petsko, G.A.4
  • 24
    • 0033595722 scopus 로고    scopus 로고
    • Identification of two serine residues involved in catalysis by fatty acid amide hydrolase
    • Omeir, R. L., G. Arreaza, and D. G. Deutsch. 1999. Identification of two serine residues involved in catalysis by fatty acid amide hydrolase. Biochem. Biophys. Res. Commun. 264:316-320.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 316-320
    • Omeir, R.L.1    Arreaza, G.2    Deutsch, D.G.3
  • 25
    • 0034705440 scopus 로고    scopus 로고
    • Clarifying the catalytic roles of conserved residues in the amidase signature family
    • Patricelli, M. P., and B. F. Cravatt. 2000. Clarifying the catalytic roles of conserved residues in the amidase signature family. J. Biol. Chem. 275:19177-19184.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19177-19184
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 26
    • 0033607236 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism
    • Patricelli, M. P., and B. F. Cravatt. 1999. Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism. Biochemistry 38:14125-14130.
    • (1999) Biochemistry , vol.38 , pp. 14125-14130
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 27
    • 0033520099 scopus 로고    scopus 로고
    • Chemical and mutagenic investigations of fatty acid amide hydrolase: Evidence for a family of serine hydrolases with distinct catalytic properties
    • Patricelli, M. P., M. A. Lovato, and B. F. Cravatt. 1999. Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties. Biochemistry 38:9804-9812.
    • (1999) Biochemistry , vol.38 , pp. 9804-9812
    • Patricelli, M.P.1    Lovato, M.A.2    Cravatt, B.F.3
  • 29
    • 0032923555 scopus 로고    scopus 로고
    • Relationships within the aldehyde dehydrogenase extended family
    • Perozich, J., H. Nicholas, B. C. Wang, R. Lindahl, and J. Hempel. 1999. Relationships within the aldehyde dehydrogenase extended family. Protein Sci. 8:137-146.
    • (1999) Protein Sci. , vol.8 , pp. 137-146
    • Perozich, J.1    Nicholas, H.2    Wang, B.C.3    Lindahl, R.4    Hempel, J.5
  • 31
    • 0024297512 scopus 로고
    • Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida
    • Ransom, S. C., J. A. Gerlt, V. M. Powers, and G. L. Kenyon. 1988. Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida. Biochemistry 27:540-545.
    • (1988) Biochemistry , vol.27 , pp. 540-545
    • Ransom, S.C.1    Gerlt, J.A.2    Powers, V.M.3    Kenyon, G.L.4
  • 32
    • 0037013923 scopus 로고    scopus 로고
    • Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature
    • Shin, S., T. H. Lee, N. C. Ha, H. M. Koo, S. Y. Kim, H. S. Lee, Y. S. Kim, and B. H. Oh. 2002. Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature. EMBO J. 21:2509-2516.
    • (2002) EMBO J. , vol.21 , pp. 2509-2516
    • Shin, S.1    Lee, T.H.2    Ha, N.C.3    Koo, H.M.4    Kim, S.Y.5    Lee, H.S.6    Kim, Y.S.7    Oh, B.H.8
  • 33
    • 0013792750 scopus 로고
    • Induction and multi-sensitive end-product repression in two converging pathways degrading aromatic substances in Pseudomonas fluorescens
    • Stevenson, I. L., and J. Mandelstam. 1965. Induction and multi-sensitive end-product repression in two converging pathways degrading aromatic substances in Pseudomonas fluorescens. Biochem. J. 96:354-362.
    • (1965) Biochem. J. , vol.96 , pp. 354-362
    • Stevenson, I.L.1    Mandelstam, J.2
  • 35
    • 0025013451 scopus 로고
    • Mandelate pathway of Pseudomonas putida: Sequence relationship involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
    • Tsou, A. Y., S. C. Ransom, J. A. Gerlt, D. D. Buechter, P. C. Babbitt, and G. L. Kenyon. 1990. Mandelate pathway of Pseudomonas putida: sequence relationship involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry 29:9856-9862.
    • (1990) Biochemistry , vol.29 , pp. 9856-9862
    • Tsou, A.Y.1    Ransom, S.C.2    Gerlt, J.A.3    Buechter, D.D.4    Babbitt, P.C.5    Kenyon, G.L.6
  • 36
    • 0024963552 scopus 로고
    • Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme
    • Tsou, A. Y., S. C. Ransom, J. A. Gerlt, V. M. Powers, and G. L. Kenyon. 1989. Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme. Biochemistry 28:969-975.
    • (1989) Biochemistry , vol.28 , pp. 969-975
    • Tsou, A.Y.1    Ransom, S.C.2    Gerlt, J.A.3    Powers, V.M.4    Kenyon, G.L.5
  • 38
    • 0014857719 scopus 로고
    • The genetic control of dissimilatory pathways in Pseudomonas putida
    • Wheelis, M. L., and R. Y. Stanier. 1970. The genetic control of dissimilatory pathways in Pseudomonas putida. Genetics 66:245-266.
    • (1970) Genetics , vol.66 , pp. 245-266
    • Wheelis, M.L.1    Stanier, R.Y.2


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