메뉴 건너뛰기




Volumn 79, Issue 10, 2013, Pages 3225-3233

Role of the phenylalanine-hydroxylating system in aromatic substance degradation and lipid metabolism in the oleaginous fungus mortierella alpina

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC SUBSTANCES; ENZYMATIC ACTIVITIES; FUNGAL DEGRADATION; GENES ENCODING ENZYMES; LIPID BIOSYNTHESIS; MORTIERELLA ALPINA; PHENYLALANINE HYDROXYLASE; TETRAHYDROBIOPTERIN;

EID: 84877157927     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00238-13     Document Type: Article
Times cited : (33)

References (74)
  • 1
    • 0000783838 scopus 로고    scopus 로고
    • Pterin-dependent amino acid hy- droxylases
    • Kappock TJ, Caradonna JP. 1996. Pterin-dependent amino acid hy- droxylases. Chem. Rev. 96:2659-2756.
    • (1996) Chem. Rev. , vol.96 , pp. 2659-2756
    • Kappock, T.J.1    Caradonna, J.P.2
  • 2
    • 35748934461 scopus 로고    scopus 로고
    • Compart- mentalization of neuronal and peripheral serotonin synthesis in Drosoph- ila melanogaster
    • Neckameyer WS, Coleman CM, Eadie S, Goodwin SF. 2007. Compart- mentalization of neuronal and peripheral serotonin synthesis in Drosoph- ila melanogaster. Genes Brain Behav. 6:756-769.
    • (2007) Genes Brain Behav , vol.6 , pp. 756-769
    • Neckameyer, W.S.1    Coleman, C.M.2    Eadie, S.3    Goodwin, S.F.4
  • 3
    • 41149168735 scopus 로고    scopus 로고
    • Correction of murine PKU following AAV-mediated intramuscular ex- pression of a complete phenylalanine hydroxylating system
    • Ding Z, Harding CO, Rebuffat A, Elzaouk L, Wolff JA, Thony B. 2008. Correction of murine PKU following AAV-mediated intramuscular ex- pression of a complete phenylalanine hydroxylating system. Mol. Ther. 16:673-681.
    • (2008) Mol. Ther. , vol.16 , pp. 673-681
    • Ding, Z.1    Harding, C.O.2    Rebuffat, A.3    Elzaouk, L.4    Wolff, J.A.5    Thony, B.6
  • 4
    • 0015193355 scopus 로고
    • The phenylalanine hydroxylating system from mam- malian liver
    • Kaufman S. 1971. The phenylalanine hydroxylating system from mam- malian liver. Adv. Enzymol. Relat. Areas Mol. Biol. 35:245-319.
    • (1971) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.35 , pp. 245-319
    • Kaufman, S.1
  • 5
    • 0036225777 scopus 로고    scopus 로고
    • Tetrahydrobiop- terin biosynthesis, utilization and pharmacological effects
    • Werner-Felmayer G, Golderer G, Werner ER. 2002. Tetrahydrobiop- terin biosynthesis, utilization and pharmacological effects. Curr. Drug Metab. 3:159-173.
    • (2002) Curr. Drug Metab. , vol.3 , pp. 159-173
    • Werner-Felmayer, G.1    Golderer, G.2    Werner, E.R.3
  • 6
    • 0034176921 scopus 로고    scopus 로고
    • Tetrahydrobiopterin biosynthesis, regeneration and functions
    • Thony B, Auerbach G, Blau N. 2000. Tetrahydrobiopterin biosynthesis, regeneration and functions. Biochem. J. 347:1-16.
    • (2000) Biochem. J. , vol.347 , pp. 1-16
    • Thony, B.1    Auerbach, G.2    Blau, N.3
  • 7
    • 0028124992 scopus 로고
    • Regulation of rat liver phenylala- nine hydroxylase
    • I. Kinetic properties of the enzyme's iron and enzyme reduction site.
    • Shiman R, Gray DW, Hill MA. 1994. Regulation of rat liver phenylala- nine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site. J. Biol. Chem. 269:24637-24646.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24637-24646
    • Shiman, R.1    Gray, D.W.2    Hill, M.A.3
  • 8
    • 0028901398 scopus 로고
    • Expression of recombinant human phenylalanine hydroxylase as fusion protein in Esch- erichia coli circumvents proteolytic degradation by host cell proteases
    • Isolation and characterization of the wild-type enzyme.
    • Martinez A, Knappskog PM, Olafsdottir S, Doskeland AP, Eiken HG, Svebak RM, Bozzini M, Apold J, Flatmark T. 1995. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Esch- erichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme. Biochem. J. 306: 589-597.
    • (1995) Biochem. J. , vol.306 , pp. 589-597
    • Martinez, A.1    Knappskog, P.M.2    Olafsdottir, S.3    Doskeland, A.P.4    Eiken, H.G.5    Svebak, R.M.6    Bozzini, M.7    Apold, J.8    Flatmark, T.9
  • 10
    • 80054757000 scopus 로고    scopus 로고
    • Microbial degradation of aromatic compounds-from one strategy to four
    • Fuchs G, Boll M, Heider J. 2011. Microbial degradation of aromatic compounds-from one strategy to four. Nat. Rev. Microbiol. 9:803-816.
    • Nat. Rev. Microbiol. , vol.9 , pp. 803-816
    • Fuchs, G.1    Boll, M.2    Heider, J.3
  • 11
    • 0028049314 scopus 로고
    • Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster
    • Zhao G, Xia T, Song J, Jensen RA. 1994. Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster. Proc. Natl. Acad. Sci. U. S. A. 91:1366-1370
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1366-1370
    • Zhao, G.1    Xia, T.2    Song, J.3    Jensen, R.A.4
  • 13
    • 34547602017 scopus 로고    scopus 로고
    • Structure of phenylalanine hydroxylase from Colwellia psychreryth- raea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability
    • Leiros HK, Pey AL, Innselset M, Moe E, Leiros I, Steen IH, Martinez A. 2007. Structure of phenylalanine hydroxylase from Colwellia psychreryth- raea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability. J. Biol. Chem. 282:21973-21986
    • (2007) J. Biol. Chem. , vol.282 , pp. 21973-21986
    • Leiros, H.K.1    Pey, A.L.2    Innselset, M.3    Moe, E.4    Leiros, I.5    Steen, I.H.6    Martinez, A.7
  • 14
    • 3242813728 scopus 로고    scopus 로고
    • The homogentisate pathway: a central catabolic pathway involved in the degradation of L-phenylalanine, L-ty- rosine, and 3-hydroxyphenylacetate in Pseudomonas putida
    • Arias-Barrau E, Olivera ER, Luengo JM, Fernandez C, Galan B, Garcia JL, Diaz E, Minambres B. 2004. The homogentisate pathway: a central catabolic pathway involved in the degradation of L-phenylalanine, L-ty- rosine, and 3-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 186:5062-5077.
    • (2004) J. Bacteriol. , vol.186 , pp. 5062-5077
    • Arias-Barrau, E.1    Olivera, E.R.2    Luengo, J.M.3    Fernandez, C.4    Galan, B.5    Garcia, J.L.6    Diaz, E.7    Minambres, B.8
  • 17
    • 0034836582 scopus 로고    scopus 로고
    • Reduced function of a phenylacetate- oxidizing cytochrome p450 caused strong genetic improvement in early phylogeny of penicillin-producing strains
    • Rodriguez-Saiz M, Barredo JL, Moreno MA, Fernandez-Canon JM, Penalva MA, Diez B. 2001. Reduced function of a phenylacetate- oxidizing cytochrome p450 caused strong genetic improvement in early phylogeny of penicillin-producing strains. J. Bacteriol. 183:5465-5471.
    • (2001) J. Bacteriol. , vol.183 , pp. 5465-5471
    • Rodriguez-Saiz, M.1    Barredo, J.L.2    Moreno, M.A.3    Fernandez-Canon, J.M.4    Penalva, M.A.5    Diez, B.6
  • 18
    • 0017103913 scopus 로고
    • Metabolism of DL- (Universal-GreekwithMathPi -1. H11001/Universal-GreekwithMathPi. -1. H11002)-phenylalanine by Aspergillus niger
    • Kishore G, Sugumaran M, Vaidyanathan CS. 1976. Metabolism of DL- (Universal-GreekwithMathPi.-1.H11001/Universal-GreekwithMathPi.-1.H11002)-phenylalanine by Aspergillus niger. J. Bacteriol. 128:182-191.
    • (1976) J. Bacteriol. , vol.128 , pp. 182-191
    • Kishore, G.1    Sugumaran, M.2    Vaidyanathan, C.S.3
  • 19
    • 0034087468 scopus 로고    scopus 로고
    • Novel scheme for biosynthesis of aryl metabolites from L-phenylalanine in the fungus Bjerkandera adusta
    • Lapadatescu C, Ginies C, Le Quere JL, Bonnarme P. 2000. Novel scheme for biosynthesis of aryl metabolites from L-phenylalanine in the fungus Bjerkandera adusta. Appl. Environ. Microbiol. 66:1517-1522.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1517-1522
    • Lapadatescu, C.1    Ginies, C.2    Le Quere, J.L.3    Bonnarme, P.4
  • 22
    • 80155164964 scopus 로고    scopus 로고
    • Biochemical characterization of the tetrahydrobiopterin synthesis pathway in the oleaginous fungus Mortier- ella alpina
    • Wang H, Yang B, Hao G, Feng Y, Chen H, Feng L, Zhao J, Zhang H, Chen YQ, Wang L, Chen W. 2011. Biochemical characterization of the tetrahydrobiopterin synthesis pathway in the oleaginous fungus Mortier- ella alpina. Microbiology 157:3059-3070.
    • (2011) Microbiology , vol.157 , pp. 3059-3070
    • Wang, H.1    Yang, B.2    Hao, G.3    Feng, Y.4    Chen, H.5    Feng, L.6    Zhao, J.7    Zhang, H.8    Chen, Y.Q.9    Wang, L.10    Chen, W.11
  • 23
    • 67649295229 scopus 로고    scopus 로고
    • Improved production of various polyunsaturated fatty acids through filamentous fungus Mor- tierella alpina breeding
    • Sakuradani E, Ando A, Ogawa J, Shimizu S. 2009. Improved production of various polyunsaturated fatty acids through filamentous fungus Mor- tierella alpina breeding. Appl. Microbiol. Biotechnol. 84:1-10.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 1-10
    • Sakuradani, E.1    Ando, A.2    Ogawa, J.3    Shimizu, S.4
  • 25
    • 0032589910 scopus 로고    scopus 로고
    • Delta6-fatty acid desatu- rase from an arachidonic acid-producing Mortierella fungus. Gene clon- ing and its heterologous expression in a fungus, Aspergillus
    • Sakuradani E, Kobayashi M, Shimizu S. 1999. Delta6-fatty acid desatu- rase from an arachidonic acid-producing Mortierella fungus. Gene clon- ing and its heterologous expression in a fungus, Aspergillus. Gene 238: 445-453.
    • (1999) Gene , vol.238 , pp. 445-453
    • Sakuradani, E.1    Kobayashi, M.2    Shimizu, S.3
  • 26
    • 0033557866 scopus 로고    scopus 로고
    • Delta 9-fatty acid desatu- rase from arachidonic acid-producing fungus. Unique gene sequence and its heterologous expression in a fungus, Aspergillus
    • Sakuradani E, Kobayashi M, Shimizu S. 1999. Delta 9-fatty acid desatu- rase from arachidonic acid-producing fungus. Unique gene sequence and its heterologous expression in a fungus, Aspergillus. Eur. J. Biochem. 260: 208-216.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 208-216
    • Sakuradani, E.1    Kobayashi, M.2    Shimizu, S.3
  • 27
    • 0033125454 scopus 로고    scopus 로고
    • Identification of Delta12-fatty acid desaturase from arachidonic acid-producing mor- tierella fungus by heterologous expression in the yeast Saccharomyces cerevisiae and the fungus Aspergillus oryzae
    • Sakuradani E, Kobayashi M, Ashikari T, Shimizu S. 1999. Identification of Delta12-fatty acid desaturase from arachidonic acid-producing mor- tierella fungus by heterologous expression in the yeast Saccharomyces cerevisiae and the fungus Aspergillus oryzae. Eur. J. Biochem. 261:812- 820.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 812-820
    • Sakuradani, E.1    Kobayashi, M.2    Ashikari, T.3    Shimizu, S.4
  • 28
    • 15244363074 scopus 로고    scopus 로고
    • A novel fungal omega3- desaturase with wide substrate specificity from arachidonic acid- producing Mortierella alpina 1S-4
    • Sakuradani E, Abe T, Iguchi K, Shimizu S. 2005. A novel fungal omega3- desaturase with wide substrate specificity from arachidonic acid- producing Mortierella alpina 1S-4. Appl. Microbiol. Biotechnol. 66:648- 654.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 648-654
    • Sakuradani, E.1    Abe, T.2    Iguchi, K.3    Shimizu, S.4
  • 29
    • 0036865034 scopus 로고    scopus 로고
    • Regulation of lipid accumulation in oleaginous micro- organisms
    • Ratledge C. 2002. Regulation of lipid accumulation in oleaginous micro- organisms. Biochem. Soc. Trans. 30:1047-1050.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1047-1050
    • Ratledge, C.1
  • 30
    • 10044264487 scopus 로고    scopus 로고
    • Fatty acid biosynthesis in microorganisms being used for single cell oil production
    • Ratledge C. 2004. Fatty acid biosynthesis in microorganisms being used for single cell oil production. Biochimie 86:807-815.
    • (2004) Biochimie , vol.86 , pp. 807-815
    • Ratledge, C.1
  • 31
    • 0036213208 scopus 로고    scopus 로고
    • Lipid status and long-chain poly- unsaturated fatty acid concentrations in adults and adolescents with phe- nylketonuria on phenylalanine-restricted diet
    • Moseley K, Koch R, Moser AB. 2002. Lipid status and long-chain poly- unsaturated fatty acid concentrations in adults and adolescents with phe- nylketonuria on phenylalanine-restricted diet. J. Inherited Metab. Dis. 25:56-64.
    • (2002) J. Inherited Metab. Dis. , vol.25 , pp. 56-64
    • Moseley, K.1    Koch, R.2    Moser, A.B.3
  • 33
    • 0027267693 scopus 로고
    • New tetrahydrobiopterin-dependent systems
    • Kaufman S. 1993. New tetrahydrobiopterin-dependent systems. Annu. Rev. Nutr. 13:261-286.
    • (1993) Annu. Rev. Nutr. , vol.13 , pp. 261-286
    • Kaufman, S.1
  • 35
  • 37
    • 84876684046 scopus 로고    scopus 로고
    • Malic enzyme activity is not the only bottleneck for lipid accumulation in the oleaginous fungus Mucor circinelloides
    • [Epub ahead of print.] doi:10.1007/s00253-012-4432-2
    • Rodriguez-Frometa RA, Gutierrez A, Torres-Martinez S, Garre V. 2012. Malic enzyme activity is not the only bottleneck for lipid accumulation in the oleaginous fungus Mucor circinelloides. Appl. Microbiol. Biotechnol. [Epub ahead of print.] doi:10.1007/s00253-012-4432-2.
    • (2012) Appl. Microbiol. Biotechnol
    • Rodriguez-Frometa, R.A.1    Gutierrez, A.2    Torres-Martinez, S.3    Garre, V.4
  • 38
    • 84855249317 scopus 로고    scopus 로고
    • Alternative routes of acetyl-CoA synthesis identified by comparative genomic analysis: involvement in the lipid production of oleaginous yeast and fungi
    • Vorapreeda T, Thammarongtham C, Cheevadhanarak S, Laoteng K. 2012. Alternative routes of acetyl-CoA synthesis identified by comparative genomic analysis: involvement in the lipid production of oleaginous yeast and fungi. Microbiology 158:217-228.
    • (2012) Microbiology , vol.158 , pp. 217-228
    • Vorapreeda, T.1    Thammarongtham, C.2    Cheevadhanarak, S.3    Laoteng, K.4
  • 40
    • 0014601365 scopus 로고
    • Irreversible in vivo inhibition of rat liver phenylalanine hydroxylase by p-chlorophenylalanine
    • Guroff G. 1969. Irreversible in vivo inhibition of rat liver phenylalanine hydroxylase by p-chlorophenylalanine. Arch. Biochem. Biophys. 134: 610-611.
    • (1969) Arch. Biochem. Biophys. , vol.134 , pp. 610-611
    • Guroff, G.1
  • 45
    • 58149185126 scopus 로고    scopus 로고
    • BRENDA AMENDA and FRENDA the enzyme information system: new content and tools in 2009
    • Chang A, Scheer M, Grote A, Schomburg I, Schomburg D. 2009. BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009. Nucleic Acids Res. 37:D588-D592.
    • (2009) Nucleic Acids Res , vol.37
    • Chang, A.1    Scheer, M.2    Grote, A.3    Schomburg, I.4    Schomburg, D.5
  • 47
    • 0026722611 scopus 로고
    • Desaturation of polyunsaturated fatty acids in Mucor circinelloides and the involvement of a novel membrane- bound malic enzyme
    • Kendrick A, Ratledge C. 1992. Desaturation of polyunsaturated fatty acids in Mucor circinelloides and the involvement of a novel membrane- bound malic enzyme. Eur. J. Biochem. 209:667-673.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 667-673
    • Kendrick, A.1    Ratledge, C.2
  • 48
    • 4944261789 scopus 로고    scopus 로고
    • Isolating Mortierella alpina strains of high yield of arachidonic acid
    • Zhu M, Yu LJ, Liu Z, Xu HB. 2004. Isolating Mortierella alpina strains of high yield of arachidonic acid. Lett. Appl. Microbiol. 39:332-335.
    • (2004) Lett. Appl. Microbiol , vol.39 , pp. 332-335
    • Zhu, M.1    Yu, L.J.2    Liu, Z.3    Xu, H.B.4
  • 51
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 52
    • 0019203132 scopus 로고
    • An assay for picomole levels of tyrosine and related phenols and its application to the measurement of phenylalanine hydroxylase activity
    • Bailey SW, Ayling JE. 1980. An assay for picomole levels of tyrosine and related phenols and its application to the measurement of phenylalanine hydroxylase activity. Anal. Biochem. 107:156-164.
    • (1980) Anal. Biochem. , vol.107 , pp. 156-164
    • Bailey, S.W.1    Ayling, J.E.2
  • 53
    • 72049121648 scopus 로고    scopus 로고
    • Determination of phenylalanine and tyrosine in plasma and dried blood samples using HPLC with fluorescence detec- tion
    • Kand'ar R, Zakova P. 2009. Determination of phenylalanine and tyrosine in plasma and dried blood samples using HPLC with fluorescence detec- tion. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 877:3926-3929
    • (2009) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.877 , pp. 3926-3929
    • Kand'ar, R.1    Zakova, P.2
  • 54
    • 0024405058 scopus 로고
    • High-level expression of human dihydropteridine reductase (EC 1.6.99.7), without N-terminal amino acid protection, in Escherichia coli
    • Armarego WL, Cotton RG, Dahl HH, Dixon NE. 1989. High-level expression of human dihydropteridine reductase (EC 1.6.99.7), without N-terminal amino acid protection, in Escherichia coli. Biochem. J. 261: 265-268.
    • (1989) Biochem. J. , vol.261 , pp. 265-268
    • Armarego, W.L.1    Cotton, R.G.2    Dahl, H.H.3    Dixon, N.E.4
  • 55
    • 0015501733 scopus 로고
    • The isolation and characterization of dihydropteridine reductase from sheep liver
    • Craine JE, Hall ES, Kaufman S. 1972. The isolation and characterization of dihydropteridine reductase from sheep liver. J. Biol. Chem. 247:6082- 6091.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6082-6091
    • Craine, J.E.1    Hall, E.S.2    Kaufman, S.3
  • 56
    • 0024413420 scopus 로고
    • Evidence for the formation of the 4a- carbinolamine during the tyrosine-dependent oxidation of tetrahydrobi- opterin by rat liver phenylalanine hydroxylase
    • Davis MD, Kaufman S. 1989. Evidence for the formation of the 4a- carbinolamine during the tyrosine-dependent oxidation of tetrahydrobi- opterin by rat liver phenylalanine hydroxylase. J. Biol. Chem. 264:8585- 8596.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8585-8596
    • Davis, M.D.1    Kaufman, S.2
  • 57
    • 0027419571 scopus 로고
    • Phenylalanine hydroxylase- stimulating protein/pterin-4 alpha-carbinolamine dehydratase from rat and human liver. Purification, characterization, and complete amino acid sequence
    • Hauer CR, Rebrin I, Thony B, Neuheiser F, Curtius HC, Hunziker P, Blau N, Ghisla S, Heizmann CW. 1993. Phenylalanine hydroxylase- stimulating protein/pterin-4 alpha-carbinolamine dehydratase from rat and human liver. Purification, characterization, and complete amino acid sequence. J. Biol. Chem. 268:4828-4831.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4828-4831
    • Hauer, C.R.1    Rebrin, I.2    Thony, B.3    Neuheiser, F.4    Curtius, H.C.5    Hunziker, P.6    Blau, N.7    Ghisla, S.8    Heizmann, C.W.9
  • 58
    • 55149093396 scopus 로고    scopus 로고
    • The phy- logeny of the aromatic amino acid hydroxylases revisited by characterizing phenylalanine hydroxylase from Dictyostelium discoideum
    • Siltberg-Liberles J, Steen IH, Svebak RM, Martinez A. 2008. The phy- logeny of the aromatic amino acid hydroxylases revisited by characterizing phenylalanine hydroxylase from Dictyostelium discoideum. Gene 427: 86-92.
    • (2008) Gene , vol.427 , pp. 86-92
    • Siltberg-Liberles, J.1    Steen, I.H.2    Svebak, R.M.3    Martinez, A.4
  • 59
    • 0023654091 scopus 로고
    • Biochemical characterization of recombinant human phenylalanine hydroxylase produced in Escherichia coli
    • Ledley FD, Grenett HE, Woo SL. 1987. Biochemical characterization of recombinant human phenylalanine hydroxylase produced in Escherichia coli. J. Biol. Chem. 262:2228-2233.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2228-2233
    • Ledley, F.D.1    Grenett, H.E.2    Woo, S.L.3
  • 60
    • 13844271849 scopus 로고    scopus 로고
    • Effect of temperature, pH, and metals on the stability and activity of phenylalanine hydroxylase from Chromobacterium violaceum
    • Zoidakis J, Loaiza B, Vu K, Abu-Omar MM. 2005. Effect of temperature, pH, and metals on the stability and activity of phenylalanine hydroxylase from Chromobacterium violaceum. J. Inorg. Biochem. 99:771-775.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 771-775
    • Zoidakis, J.1    Loaiza, B.2    Vu, K.3    Abu-Omar, M.M.4
  • 61
    • 67349153702 scopus 로고    scopus 로고
    • Iron binding effects on the kinetic stability and unfolding energetics of a thermophilic phenylalanine hydroxylase from Chloroflexus aurantiacus
    • Pey AL, Martinez A. 2009. Iron binding effects on the kinetic stability and unfolding energetics of a thermophilic phenylalanine hydroxylase from Chloroflexus aurantiacus. J. Biol. Inorg. Chem. 14:521-531.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 521-531
    • Pey, A.L.1    Martinez, A.2
  • 62
    • 0034981940 scopus 로고    scopus 로고
    • Missense muta- tions in the N-terminal domain of human phenylalanine hydroxylase in- terfere with binding of regulatory phenylalanine
    • Gjetting T, Petersen M, Guldberg P, Guttler F. 2001. Missense muta- tions in the N-terminal domain of human phenylalanine hydroxylase in- terfere with binding of regulatory phenylalanine. Am. J. Hum. Genet. 68:1353-1360.
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 1353-1360
    • Gjetting, T.1    Petersen, M.2    Guldberg, P.3    Guttler, F.4
  • 63
    • 0035941096 scopus 로고    scopus 로고
    • High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobi- opterin
    • Andersen OA, Flatmark T, Hough E. 2001. High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobi- opterin. J. Mol. Biol. 314:279-291.
    • (2001) J. Mol. Biol. , vol.314 , pp. 279-291
    • Andersen, O.A.1    Flatmark, T.2    Hough, E.3
  • 64
    • 0036071847 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydrox- ylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its impli- cations for the mechanism of catalysis and substrate activation
    • Andersen OA, Flatmark T, Hough E. 2002. Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydrox- ylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its impli- cations for the mechanism of catalysis and substrate activation. J. Mol. Biol. 320:1095-1108.
    • (2002) J. Mol. Biol. , vol.320 , pp. 1095-1108
    • Andersen, O.A.1    Flatmark, T.2    Hough, E.3
  • 65
    • 0036310665 scopus 로고    scopus 로고
    • Structural comparison of bacterial and human iron- dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates
    • Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC. 2002. Structural comparison of bacterial and human iron- dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. J. Mol. Biol. 320:645-661.
    • (2002) J. Mol. Biol. , vol.320 , pp. 645-661
    • Erlandsen, H.1    Kim, J.Y.2    Patch, M.G.3    Han, A.4    Volner, A.5    Abu-Omar, M.M.6    Stevens, R.C.7
  • 67
    • 0032479302 scopus 로고    scopus 로고
    • Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria
    • Fusetti F, Erlandsen H, Flatmark T, Stevens RC. 1998. Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J. Biol. Chem. 273:16962-16967.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16962-16967
    • Fusetti, F.1    Erlandsen, H.2    Flatmark, T.3    Stevens, R.C.4
  • 68
    • 0034093759 scopus 로고    scopus 로고
    • Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hy- droxylase
    • Erlandsen H, Bjorgo E, Flatmark T, Stevens RC. 2000. Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hy- droxylase. Biochemistry 39:2208-2217.
    • (2000) Biochemistry , vol.39 , pp. 2208-2217
    • Erlandsen, H.1    Bjorgo, E.2    Flatmark, T.3    Stevens, R.C.4
  • 70
    • 0034948274 scopus 로고    scopus 로고
    • Role of nitric oxide synthase in the light-induced development of sporangiophores in Phyco- myces blakesleeanus
    • Maier J, Hecker R, Rockel P, Ninnemann H. 2001. Role of nitric oxide synthase in the light-induced development of sporangiophores in Phyco- myces blakesleeanus. Plant Physiol. 126:1323-1330.
    • (2001) Plant Physiol , vol.126 , pp. 1323-1330
    • Maier, J.1    Hecker, R.2    Rockel, P.3    Ninnemann, H.4
  • 71
    • 0030221435 scopus 로고    scopus 로고
    • Indications for the occurrence of nitric oxide synthases in fungi and plants and the involvement in photoconidi- ation of Neurospora crassa
    • Ninnemann H, Maier J. 1996. Indications for the occurrence of nitric oxide synthases in fungi and plants and the involvement in photoconidi- ation of Neurospora crassa. Photochem. Photobiol. 64:393-398.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 393-398
    • Ninnemann, H.1    Maier, J.2
  • 72
    • 34447550704 scopus 로고    scopus 로고
    • Malic enzyme: the controlling activity for lipid production? Overexpression of malic enzyme in Mucor circinelloides leads to a 2
    • Zhang Y, Adams IP, Ratledge C. 2007. Malic enzyme: the controlling activity for lipid production? Overexpression of malic enzyme in Mucor circinelloides leads to a 2.5-fold increase in lipid accumulation. Microbi- ology 153:2013-2025.
    • (2007) 5-fold increase in lipid accumulation. Microbi- ology , vol.153 , pp. 2013-2025
    • Zhang, Y.1    Adams, I.P.2    Ratledge, C.3
  • 73
    • 0032870365 scopus 로고    scopus 로고
    • The role of malic enzyme in the regulation of lipid accumulation in filamentous fungi
    • Wynn JP, bin Abdul Hamid A, Ratledge C. 1999. The role of malic enzyme in the regulation of lipid accumulation in filamentous fungi. Mi- crobiology 145:1911-1917.
    • (1999) Mi- crobiology , vol.145 , pp. 1911-1917
    • Wynn, J.P.1    bin Abdul Hamid, A.2    Ratledge, C.3
  • 74
    • 36348956692 scopus 로고    scopus 로고
    • DGA1 (diacylglycerol acyltransferase gene) overexpression and leucine biosyn- thesis significantly increase lipid accumulation in the Deltasnf2 disruptant of Saccharomyces cerevisiae
    • Kamisaka Y, Tomita N, Kimura K, Kainou K, Uemura H. 2007. DGA1 (diacylglycerol acyltransferase gene) overexpression and leucine biosyn- thesis significantly increase lipid accumulation in the Deltasnf2 disruptant of Saccharomyces cerevisiae. Biochem. J. 408:61-68
    • (2007) Biochem. J. , vol.408 , pp. 61-68
    • Kamisaka, Y.1    Tomita, N.2    Kimura, K.3    Kainou, K.4    Uemura, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.