메뉴 건너뛰기




Volumn 97, Issue 2, 2013, Pages 599-609

Advances in the bioconversion mechanism of lovastatin to wuxistatin by Amycolatopsis sp. CGMCC 1149

Author keywords

Biconversion; Cytochrome P450; Hydroxylation; Lovastatin; Product I; Wuxistatin

Indexed keywords

BICONVERSION; CELL-FREE SYSTEM; CYTOCHROME P450; FERMENTATION BROTHS; GTP-BINDING PROTEINS; HYDROXYL GROUPS; HYDROXYLASES; HYDROXYLATION REACTIONS; INTEGRAL MEMBRANE PROTEINS; INTERMEDIATE PRODUCT; INTRAMOLECULAR TRANSFER; ISOMERASES; ISOTOPE TRACING; LOVASTATIN; METHYL GROUP; OXIDOREDUCTASES; PROTEOMICS; STRUCTURE ANALYSIS; WUXISTATIN;

EID: 84873988486     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4341-4     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 16644400625 scopus 로고    scopus 로고
    • The discovery and development of HMG-CoA reductase inhibitors
    • Akira E (2004) The discovery and development of HMG-CoA reductase inhibitors. Atheroscler Suppl 33:67-80
    • (2004) Atheroscler Suppl , vol.33 , pp. 67-80
    • Akira, E.1
  • 3
    • 0031018138 scopus 로고    scopus 로고
    • An iron-regulated outer-membrane protein specific to Bordetella bronchiseptica and homologous to ferric siderophore receptors
    • 10.1099/00221287-143-1-135 1:CAS:528:DyaK2sXptFentg%3D%3D
    • Beall B, Hoenes T (1997) An iron-regulated outer-membrane protein specific to Bordetella bronchiseptica and homologous to ferric siderophore receptors. Microbiol 143:135-145
    • (1997) Microbiol , vol.143 , pp. 135-145
    • Beall, B.1    Hoenes, T.2
  • 4
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • 10.1016/S0969-2126(02)00882-1 1:CAS:528:DC%2BD38XoslGntL4%3D
    • Buglino J, Shen V, Hakimian P, Lima CD (2002) Structural and biochemical analysis of the Obg GTP binding protein. Structure 10:1581-1592
    • (2002) Structure , vol.10 , pp. 1581-1592
    • Buglino, J.1    Shen, V.2    Hakimian, P.3    Lima, C.D.4
  • 5
    • 0032956961 scopus 로고    scopus 로고
    • Natural statins and stroke risk
    • 10.1161/01.CIR.99.2.185 1:STN:280:DyaK1M7htVOitA%3D%3D
    • Furberg CD (1999) Natural statins and stroke risk. Circulation 99:185-188
    • (1999) Circulation , vol.99 , pp. 185-188
    • Furberg, C.D.1
  • 6
    • 30544450531 scopus 로고    scopus 로고
    • Pharmacogenomics of cholesterol-lowering therapy
    • 10.1016/j.vph.2005.07.012
    • Gerd S, Thomas L (2006) Pharmacogenomics of cholesterol-lowering therapy. Vasc Pharmacol 44:75-89
    • (2006) Vasc Pharmacol , vol.44 , pp. 75-89
    • Gerd, S.1    Thomas, L.2
  • 8
    • 44249098959 scopus 로고    scopus 로고
    • Cytochrome P450 omega hydroxylase (CYP4) function in fatty acid metabolism and metabolic diseases
    • 10.1016/j.bcp.2008.03.004 1:CAS:528:DC%2BD1cXmsFKqsbs%3D
    • Hardwick JP (2008) Cytochrome P450 omega hydroxylase (CYP4) function in fatty acid metabolism and metabolic diseases. Biochem Pharmacol 75:2263-2275
    • (2008) Biochem Pharmacol , vol.75 , pp. 2263-2275
    • Hardwick, J.P.1
  • 10
    • 0032983057 scopus 로고    scopus 로고
    • Recent advances in applied and mechanistic aspects of the enzymatic hydroxylation of steroids by whole-cell biocatalysts
    • 10.1016/S0039-128X(98)00085-3 1:CAS:528:DyaK1MXktFKgt7Y%3D
    • Holland HL (1999) Recent advances in applied and mechanistic aspects of the enzymatic hydroxylation of steroids by whole-cell biocatalysts. Steroids 64:178-186
    • (1999) Steroids , vol.64 , pp. 178-186
    • Holland, H.L.1
  • 11
    • 0033635584 scopus 로고    scopus 로고
    • Enzymatic hydroxylation reactions
    • 10.1016/S0958-1669(00)00142-7 1:CAS:528:DC%2BD3MXisFGq
    • Holland HL, Weber HK (2000) Enzymatic hydroxylation reactions. Curr Opin Biotechnol 11:547-553
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 547-553
    • Holland, H.L.1    Weber, H.K.2
  • 12
    • 0031856358 scopus 로고    scopus 로고
    • Microbial hydroxylation of acetylamino-steroids
    • 10.1016/S0039-128X(98)00053-1 1:CAS:528:DyaK1cXlsFClsL4%3D
    • Holland HL, Lakshmaiah G, Ruddock PL (1998) Microbial hydroxylation of acetylamino-steroids. Steroids 63:484-495
    • (1998) Steroids , vol.63 , pp. 484-495
    • Holland, H.L.1    Lakshmaiah, G.2    Ruddock, P.L.3
  • 15
    • 0035788799 scopus 로고    scopus 로고
    • Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition
    • 10.1046/j.1365-2958.2001.02574.x 1:CAS:528:DC%2BD3MXntlGhs7Y%3D
    • Kobayashi G, Moriya S, Wada C (2001) Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition. Mol Microbiol 41(5):1037-1051
    • (2001) Mol Microbiol , vol.41 , Issue.5 , pp. 1037-1051
    • Kobayashi, G.1    Moriya, S.2    Wada, C.3
  • 16
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • 10.1093/emboj/cdg598 1:CAS:528:DC%2BD3sXpvVemsLc%3D
    • Layer G, Moser J, Heinz DW, Jahn D, Schubert WD (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J 22:6214-6224
    • (2003) EMBO J , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 17
    • 18844469113 scopus 로고    scopus 로고
    • Production of lovastatin by Aspergillus terreus: Effects of the C:N ratio and the principal nutrients on growth and metabolite production
    • 10.1016/S0141-0229(03)00130-3
    • Lopez JLC, Perez JAS, Sevilla JMF, Fernandez FGA, Grima EM, Chisti Y (2003) Production of lovastatin by Aspergillus terreus: effects of the C:N ratio and the principal nutrients on growth and metabolite production. Enzyme Microb Technol 33:270-277
    • (2003) Enzyme Microb Technol , vol.33 , pp. 270-277
    • Lopez, J.L.C.1    Perez, J.A.S.2    Sevilla, J.M.F.3    Fernandez, F.G.A.4    Grima, E.M.5    Chisti, Y.6
  • 18
    • 34247513942 scopus 로고    scopus 로고
    • From the genome sequence to the proteome and back: Evaluation of E. coli genome annotation with a 2-D gel-based proteomics approach
    • 10.1002/pmic.200600599 1:CAS:528:DC%2BD2sXksFSluro%3D
    • Maillet I, Berndt P, Malo C, Rodriguez S, Brunisholz RA, Pragai Z, Arnold S, Langen H, Wyss M (2007) From the genome sequence to the proteome and back: evaluation of E. coli genome annotation with a 2-D gel-based proteomics approach. Proteomics 7:1097-1106
    • (2007) Proteomics , vol.7 , pp. 1097-1106
    • Maillet, I.1    Berndt, P.2    Malo, C.3    Rodriguez, S.4    Brunisholz, R.A.5    Pragai, Z.6    Arnold, S.7    Langen, H.8    Wyss, M.9
  • 19
    • 0036222207 scopus 로고    scopus 로고
    • Biosynthesis and biotechnological production of statins by filamentous fungi and application of these cholesterol-lowering drugs
    • 10.1007/s00253-002-0932-9 1:CAS:528:DC%2BD38Xjs12ktL0%3D
    • Manzoni M, Rollini M (2002) Biosynthesis and biotechnological production of statins by filamentous fungi and application of these cholesterol-lowering drugs. Appl Microbiol Biotechnol 58:555-564
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 555-564
    • Manzoni, M.1    Rollini, M.2
  • 20
    • 14244251991 scopus 로고    scopus 로고
    • Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin
    • 10.1042/BJ20040490 1:CAS:528:DC%2BD2MXhtFWmtrg%3D
    • Mendes MV, Anton N, Martin JF, Aparicio JF (2005) Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin. Biochem J 386:57-62
    • (2005) Biochem J , vol.386 , pp. 57-62
    • Mendes, M.V.1    Anton, N.2    Martin, J.F.3    Aparicio, J.F.4
  • 21
    • 0038559504 scopus 로고    scopus 로고
    • Bacterial conversion of hydroxylamino aromatic compounds by both lyase and mutase enzymes involves intramolecular transfer of hydroxyl groups
    • 10.1128/AEM.69.5.2786-2793.2003 1:CAS:528:DC%2BD3sXjslOlsbg%3D
    • Nadeau LJ, He ZQ, Spain JC (2003) Bacterial conversion of hydroxylamino aromatic compounds by both lyase and mutase enzymes involves intramolecular transfer of hydroxyl groups. Appl Environ Microbiol 69:2786-2793
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2786-2793
    • Nadeau, L.J.1    He, Z.Q.2    Spain, J.C.3
  • 22
    • 0028850367 scopus 로고
    • Structure and function of microbial iron transport compounds
    • 1:CAS:528:DyaK2MXpsVGmurw%3D
    • Neilands JB (1995) Structure and function of microbial iron transport compounds. J Biol Chem 270:26723-26726
    • (1995) J Biol Chem , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 23
    • 0034605585 scopus 로고    scopus 로고
    • Bioconversion of compactin to pravastatin by Actinomadura sp. ATCC 55678
    • 10.1016/S1381-1177(00)00123-5 1:CAS:528:DC%2BD3cXltVGqsrY%3D
    • Peng Y, Demain AL (2000) Bioconversion of compactin to pravastatin by Actinomadura sp. ATCC 55678. J Mol Catal B: Enzym 10:151-156
    • (2000) J Mol Catal B: Enzym , vol.10 , pp. 151-156
    • Peng, Y.1    Demain, A.L.2
  • 24
    • 0032765908 scopus 로고    scopus 로고
    • Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma (B)
    • 1:CAS:528:DyaK1MXkvFCitbw%3D
    • Scott JM, Haldenwang WG (1999) Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma (B). J Bacterial 181(15):4653-4660
    • (1999) J Bacterial , vol.181 , Issue.15 , pp. 4653-4660
    • Scott, J.M.1    Haldenwang, W.G.2
  • 25
    • 0025767694 scopus 로고
    • A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • 10.1016/0005-2760(91)90052-J 1:CAS:528:DyaK3MXkvVOqu7k%3D
    • Serizawa N, Matsuoka T (1991) A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase. BBA 1084:35-40
    • (1991) BBA , vol.1084 , pp. 35-40
    • Serizawa, N.1    Matsuoka, T.2
  • 26
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • 10.1093/nar/29.5.1097 1:CAS:528:DC%2BD3MXhvFaqsLw%3D
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29:1097-1106
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 27
    • 0029133802 scopus 로고
    • Cloning, characterization and expression of the gene encoding cytochrome P-450sca-2 from Streptomyces carbophilus involved in the production of pravastatin, a specific HMG-CoA reductase inhibitor
    • 10.1016/0378-1119(95)00394-L 1:CAS:528:DyaK2MXosVOhurs%3D
    • Watanabe I, Nara F, Serizawa N (1995) Cloning, characterization and expression of the gene encoding cytochrome P-450sca-2 from Streptomyces carbophilus involved in the production of pravastatin, a specific HMG-CoA reductase inhibitor. Gene 163:81-85
    • (1995) Gene , vol.163 , pp. 81-85
    • Watanabe, I.1    Nara, F.2    Serizawa, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.