메뉴 건너뛰기




Volumn 95, Issue 2, 2012, Pages 431-440

L-Pantoyl lactone dehydrogenase from Rhodococcus erythropolis: Genetic analyses and application to the stereospecific oxidation of L-pantoyl lactone

Author keywords

Ketopantoyl lactone; L Pantoyl lactone dehydrogenase; Rhodococcus erythropolis; Stereoinversion

Indexed keywords

1 ,2-PROPANEDIOL; AMINO ACID RESIDUES; AMINO ACID SEQUENCE; CONVERSION YIELD; GENETIC ANALYSIS; HOMOLOGY SEARCH; HYDROXY ACIDS; KETOPANTOYL LACTONE; L-PANTOYL LACTONE DEHYDROGENASE; MEMBRANE-BOUND; N-TERMINAL AMINO ACID SEQUENCE; OVER-EXPRESSION; RHODOCOCCUS ERYTHROPOLIS; STEREOINVERSION; STEREOSPECIFIC; SUBSTRATE CONCENTRATIONS; UPSTREAM REGION; WILD-TYPE STRAIN;

EID: 84864697252     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-3970-y     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0033637451 scopus 로고    scopus 로고
    • Dynamic resolution and stereoinversion of secondary alcohols by chemo-enzymatic processes
    • Azerad R, Buisson D (2000) Dynamic resolution and stereoinversion of secondary alcohols by chemo-enzymatic processes. Curr Opin Biotechnol 11:565-571
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 565-571
    • Azerad, R.1    Buisson, D.2
  • 2
    • 13444283567 scopus 로고    scopus 로고
    • Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase
    • DOI 10.1021/bi048616e
    • Cunane LM, Barton JD, Chen ZW, Le KH, Amar D, Lederer F, Mathews FS (2005) Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase. Biochemistry 44:1521-1531 (Pubitemid 40204395)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1521-1531
    • Cunane, L.M.1    Barton, J.D.2    Chen, Z.-W.3    Le, K.H.D.4    Amar, D.5    Lederer, F.6    Mathews, F.S.7
  • 3
    • 0025786780 scopus 로고
    • Amino acid sequence of long chain alpha-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent alpha-hydroxy acid-oxidizing enzymes
    • Diêp Lê KH, Lederer F (1991) Amino acid sequence of long chain α- hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes. J Biol Chem 266:20877-20881 (Pubitemid 21908545)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.31 , pp. 20877-20881
    • Le, K.H.D.1    Lederer, F.2
  • 4
    • 0035802951 scopus 로고    scopus 로고
    • Non-sequential processes for the transformation of a racemate into a single stereoisomeric product: Proposal for stereochemical classification
    • DOI 10.1002/1521-3765(20011203)7:23<5004::AID-CHEM5004>3.0.CO;2-X
    • Faber K (2001) Non-sequential processes for the transformation of a racemate into a single stereoisomeric product: proposal for stereochemical classification. Chemistry 7:5004-5010 (Pubitemid 34555630)
    • (2001) Chemistry - A European Journal , vol.7 , Issue.23 , pp. 5004-5010
    • Faber, K.1
  • 5
    • 16244380464 scopus 로고    scopus 로고
    • New enzymes for biotransformations
    • DOI 10.1016/j.cbpa.2005.01.001, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • Faber K, Kroutil W (2005) New enzymes for biotransformations. Curr Opin Chem Biol 9:181-187 (Pubitemid 40462488)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 181-187
    • Faber, K.1    Kroutil, W.2
  • 8
    • 33749323628 scopus 로고    scopus 로고
    • From a racemate to a single enantiomer: Deracemization by stereoinversion
    • DOI 10.1002/adsc.200606158
    • Gruber CG, Lavandera I, Faber K, Kroutil W (2006) From a racemate to a single enantiomer: deracemization by stereoinversion. Adv Synth Catal 348:1789-1805 (Pubitemid 44497136)
    • (2006) Advanced Synthesis and Catalysis , vol.348 , Issue.14 , pp. 1789-1805
    • Gruber, C.C.1    Lavandera, I.2    Faber, K.3    Kroutil, W.4
  • 9
    • 0026596315 scopus 로고
    • Development of a host-vector system in a Rhodococcus strain and its use for expression of the cloned nitrile hydratase gene cluster
    • Hashimoto Y, Nishiyama M, Yu F, Watanabe I, Horinouchi S, Beppu T (1992) Development of a host-vector system in a Rhodococcus strain and its use for expression of the cloned nitrile hydratase gene cluster. J Gen Microbiol 138:1003-1010
    • (1992) J Gen Microbiol , vol.138 , pp. 1003-1010
    • Hashimoto, Y.1    Nishiyama, M.2    Yu, F.3    Watanabe, I.4    Horinouchi, S.5    Beppu, T.6
  • 10
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • DOI 10.1016/0378-1119(89)90359-4
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68 (Pubitemid 19125654)
    • (1989) Gene , vol.77 , Issue.1 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 11
    • 0026516760 scopus 로고
    • Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L- (+)-pantoyl lactone dehydrogenase from Nocardia asteroides
    • Kataoka M, Shimizu S, Yamada H (1992) Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L- (+)-pantoyl lactone dehydrogenase from Nocardia asteroides. Eur J Biochem 204:799-806
    • (1992) Eur J Biochem , vol.204 , pp. 799-806
    • Kataoka, M.1    Shimizu, S.2    Yamada, H.3
  • 12
    • 0029585849 scopus 로고
    • Lactonohydrolase-catalyzed optical resolution of pantoyl lactone: Selection of a potent enzyme producer and optimization of culture and reaction conditions for practical resolution
    • DOI 10.1007/s002530050563
    • Kataoka M, Shimizu K, Sakamoto K, Yamada H, Shimizu S (1995a) Lactonohydrolase-catalyzed optical resolution of pantoyl lactone: selection of a potent enzyme producer and optimization of culture and reaction conditions for practical resolution. Appl Microbiol Biotechnol 44:333-338 (Pubitemid 26027059)
    • (1995) Applied Microbiology and Biotechnology , vol.44 , Issue.3-4 , pp. 333-338
    • Kataoka, M.1    Shimizu, K.2    Sakamoto, K.3    Yamada, H.4    Shimizu, S.5
  • 13
  • 14
    • 0030248397 scopus 로고    scopus 로고
    • Optical resolution of racemic pantoic acid through microbial stereoselective lactonization in an organic solvent/water two-phase system
    • DOI 10.1016/0141-0229(95)00250-2
    • Kataoka M, Hirakata M, Sakamoto K, Yamada H, Shimizu S (1996) Optical resolution of racemic pantoic acid through microbial stereoselective lactonization in an organic solvent/water twophase system. Enzyme Microb Technol 19:307-310 (Pubitemid 26293744)
    • (1996) Enzyme and Microbial Technology , vol.19 , Issue.4 , pp. 307-310
    • Kataoka, M.1    Hirakata, M.2    Sakamoto, K.3    Yamada, H.4    Shimizu, S.5
  • 16
    • 2442587513 scopus 로고    scopus 로고
    • Gene cloning and overexpression of two conjucated polyketone reductases, novel aldo-keto reductase family enzymes, of Candida parapsilosis
    • DOI 10.1007/s00253-003-1484-3
    • Kataoka M, Delacruz-Hidalgo AR, Akond MA, Sakuradani E, Kita K, Shimizu S (2004) Gene cloning and overexpression of two conjugated polyketone reductases, novel aldo-keto reductase family enzymes, of Candida parapsilosis. Appl Microbiol Biotechnol 64:359-366 (Pubitemid 38626460)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.3 , pp. 359-366
    • Kataoka, M.1    Delacruz-Hidalgo, A.-R.G.2    Akond, M.A.3    Sakuradani, E.4    Kita, K.5    Shimizu, S.6
  • 17
    • 0346638531 scopus 로고    scopus 로고
    • Development of a novel biocatalyst for the resolution of rac-pantolactone
    • Kesseler M, Friedrich T, Höffken HW, Hauer B (2002) Development of a novel biocatalyst for the resolution of rac-pantolactone. Adv Synth Catal 344:1103-1110
    • (2002) Adv Synth Catal , vol.344 , pp. 1103-1110
    • Kesseler, M.1    Friedrich, T.2    Höffken, H.W.3    Hauer, B.4
  • 18
    • 0016237010 scopus 로고
    • Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase
    • King HL Jr, Dyar RE, Wilken DR (1974) Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J Biol Chem 249:4689-4695
    • (1974) J Biol Chem , vol.249 , pp. 4689-4695
    • King Jr., H.L.1    Dyar, R.E.2    Wilken, D.R.3
  • 19
    • 0028817797 scopus 로고
    • L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme
    • Maeda-Yorita K, Aki K, Sagai H, Misaki H, Massey V (1995) L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme. Biochimie 77:631-642
    • (1995) Biochimie , vol.77 , pp. 631-642
    • Maeda-Yorita, K.1    Aki, K.2    Sagai, H.3    Misaki, H.4    Massey, V.5
  • 21
    • 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
    • DOI 10.1021/bi00211a003
    • Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA (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 (Pubitemid 24005900)
    • (1993) Biochemistry , vol.32 , Issue.48 , 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
    • 20444439537 scopus 로고    scopus 로고
    • Practical resolution system for DL-pantoyl lactone using the lactonase from Fusarium oxysporum
    • DOI 10.1016/j.jbiotec.2005.03.015, PII S016816560500129X
    • Sakamoto K, Honda K, Wada K, Kita S, Tsuzaki K, Nose H, Kataoka M, Shimizu S (2005) Practical resolution system for DL-pantoyl lactone using the lactonase from Fusarium oxysporum. J Biotechnol 118:99-106 (Pubitemid 40814538)
    • (2005) Journal of Biotechnology , vol.118 , Issue.1 , pp. 99-106
    • Sakamoto, K.1    Honda, K.2    Wada, K.3    Kita, S.4    Tsuzaki, K.5    Nose, H.6    Kataoka, M.7    Shimizu, S.8
  • 25
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • DOI 10.1016/0378-1119(94)90324-7
    • Schafer A, Tauch A, Jager W, Kalinowski J, Thierbach G, Puhler A (1994) Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73 (Pubitemid 24224965)
    • (1994) Gene , vol.145 , Issue.1 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5    Puhler, A.6
  • 27
    • 0023146655 scopus 로고
    • One-step microbial conversion of a racemic mixture of pantoyl lactone to optically active D-(-)-pantoyl lactone
    • Shimizu S, Hattori S, Hata H, Yamada H (1987) One-step microbial conversion of a racemic mixture of pantoyl lactone to optically active D-(-)-pantoyl lactone. Appl Environ Microbiol 53:519-522 (Pubitemid 17017541)
    • (1987) Applied and Environmental Microbiology , vol.53 , Issue.3 , pp. 519-522
    • Shimizu, S.1    Hattori, S.2    Hata, H.3    Yamada, H.4
  • 28
    • 0026699044 scopus 로고
    • Purification and characterization of a novel lactonohydrolase, catalyzing the hydrolysis of aldonate lactones and aromatic lactones, from Fusarium oxysporum
    • Shimizu S, Kataoka M, Shimizu K, Hirakata M, Sakamoto K, Yamada H (1992) Purification and characterization of a novel lactonohydrolase, catalyzing the hydrolysis of aldonate lactones and aromatic lactones, from Fusarium oxysporum. Eur J Biochem 209:383-390
    • (1992) Eur J Biochem , vol.209 , pp. 383-390
    • Shimizu, S.1    Kataoka, M.2    Shimizu, K.3    Hirakata, M.4    Sakamoto, K.5    Yamada, H.6
  • 29
    • 84857922396 scopus 로고    scopus 로고
    • Cloning and overexpression of ketopantoic acid reductase gene from Stenotrophomonas maltophilia and its application to stereospecific production of D-pantoic acid
    • Si D, Urano N, Shimizu S, Kataoka M (2012) Cloning and overexpression of ketopantoic acid reductase gene from Stenotrophomonas maltophilia and its application to stereospecific production of D-pantoic acid. Appl Microbiol Biotechnol 93:1619-1625
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 1619-1625
    • Si, D.1    Urano, N.2    Shimizu, S.3    Kataoka, M.4
  • 30
    • 0031049952 scopus 로고    scopus 로고
    • Biocatalytic deracemization techniques: Dynamic resolutions and stereoinversions
    • Stecher H, Faber K (1997) Biocatalytic deracemization techniques: dynamic resolutions and stereoinversions. Synthesis 1997:1-16 (Pubitemid 27089118)
    • (1997) Synthesis , Issue.1 , pp. 1-16
    • Stecher, H.1    Faber, K.2
  • 31
    • 0033556602 scopus 로고    scopus 로고
    • Biocatalytic transformation of racemates into chiral building blocks in 100% chemical yield and 100% enantiomeric excess
    • DOI 10.1016/S0957-4166(98)00490-X, PII S095741669800490X
    • Strauss UT, Felfer U, Faber K (1999) Biocatalytic transformation of racemates into chiral building blocks in 100% chemical yield and 100% enantiomeric excess. Tetrahedron: Asymmetry 10:107-117 (Pubitemid 29089210)
    • (1999) Tetrahedron Asymmetry , vol.10 , Issue.1 , pp. 107-117
    • Strauss, U.T.1    Felfer, U.2    Faber, K.3
  • 32
    • 0035928723 scopus 로고    scopus 로고
    • Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase
    • DOI 10.1021/bi010938k
    • Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS (2001) Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase. Biochemistry 40:9870-9878 (Pubitemid 32769535)
    • (2001) Biochemistry , vol.40 , Issue.33 , pp. 9870-9878
    • Sukumar, N.1    Xu, Y.2    Gatti, D.L.3    Mitra, B.4    Mathews, F.S.5
  • 33
    • 79251598466 scopus 로고    scopus 로고
    • Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: A putative GntR transcription factor in transcriptional regulation
    • Urano N, Kataoka M, Ishige T, Kita S, Sakamoto K, Shimizu S (2011) Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: a putative GntR transcription factor in transcriptional regulation. Appl Microbiol Biotechnol 89:739-746
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 739-746
    • Urano, N.1    Kataoka, M.2    Ishige, T.3    Kita, S.4    Sakamoto, K.5    Shimizu, S.6
  • 34
    • 0025278264 scopus 로고
    • Molecular structure of flavocytochrome b2 at 2.4 Å resolution
    • Xia ZX, Mathews FS (1990) Molecular structure of flavocytochrome b2 at 2.4 Å resolution. J Mol Biol 212:837-863
    • (1990) J Mol Biol , vol.212 , pp. 837-863
    • Xia, Z.X.1    Mathews, F.S.2
  • 35
    • 54449092486 scopus 로고    scopus 로고
    • Discovery of posttranslational maturation by self-subunit swapping
    • Zhou Z, Hashimoto Y, Shiraki K, Kobayashi M (2008) Discovery of posttranslational maturation by self-subunit swapping. Proc Natl Acad Sci USA 105:14849-14854
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14849-14854
    • Zhou, Z.1    Hashimoto, Y.2    Shiraki, K.3    Kobayashi, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.