메뉴 건너뛰기




Volumn 586, Issue 23, 2012, Pages 4228-4232

Identification of a HAD superfamily phosphatase, HdpA, involved in 1,3-dihydroxyacetone production during sugar catabolism in Corynebacterium glutamicum

Author keywords

1,3 Dihydroxyacetone; Corynebacterium glutamicum; Dihydroxyacetone phosphatase; Haloacid dehalogenase superfamily

Indexed keywords

1,3 DIHYDROXYACETONE; DIHYDROXYACETONE; DIHYDROXYACETONE PHOSPHATE; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; FRUCTOSE; GLUCOSE; HALOACID DEHALOGENASE PHOSPHATASE; PHOSPHATASE; PROTEIN HDPA; SUCROSE; UNCLASSIFIED DRUG;

EID: 84869504360     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.10.028     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 44749083834 scopus 로고    scopus 로고
    • Microbial production of dihydroxyacetone
    • R. Mishra, S.R. Jain, and A. Kumar Microbial production of dihydroxyacetone Biotechnol. Adv. 26 2008 293 303
    • (2008) Biotechnol. Adv. , vol.26 , pp. 293-303
    • Mishra, R.1    Jain, S.R.2    Kumar, A.3
  • 2
    • 0037210588 scopus 로고    scopus 로고
    • Biochemistry and biotechnological applications of Gluconobacter strains
    • U. Deppenmeier, M. Hoffmeister, and C. Prust Biochemistry and biotechnological applications of Gluconobacter strains Appl. Microbiol. Biotechnol. 60 2002 233 242
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 233-242
    • Deppenmeier, U.1    Hoffmeister, M.2    Prust, C.3
  • 3
    • 0019126232 scopus 로고
    • Pentose phosphate-dependent fixation of formaldehyde by methanol-grown Hansenula polymorpha and Candida boidinii
    • M. O'Connor, and J. Quayle Pentose phosphate-dependent fixation of formaldehyde by methanol-grown Hansenula polymorpha and Candida boidinii J. Gen. Microbiol. 120 1980 219
    • (1980) J. Gen. Microbiol. , vol.120 , pp. 219
    • O'Connor, M.1    Quayle, J.2
  • 4
    • 0022588218 scopus 로고
    • Dihydroxyacetone production from methanol by a dihydroxyacetone kinase deficient mutant of Hansenula polymorpha
    • N. Kato, H. Kobayashi, M. Shimao, and C. Sakazawa Dihydroxyacetone production from methanol by a dihydroxyacetone kinase deficient mutant of Hansenula polymorpha Appl. Microbiol. Biotechnol. 23 1986 180 186
    • (1986) Appl. Microbiol. Biotechnol. , vol.23 , pp. 180-186
    • Kato, N.1    Kobayashi, H.2    Shimao, M.3    Sakazawa, C.4
  • 5
  • 6
    • 0028228634 scopus 로고
    • Enzymes involved in the formation of glycerol 3-phosphate and the by-products dihydroxyacetone and glycerol in Zymomonas mobilis
    • S. Horbach, J. Strohhacker, R. Welle, A. de Graaf, and H. Sahm Enzymes involved in the formation of glycerol 3-phosphate and the by-products dihydroxyacetone and glycerol in Zymomonas mobilis FEMS Microbiol. Lett. 120 1994 37 44
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 37-44
    • Horbach, S.1    Strohhacker, J.2    Welle, R.3    De Graaf, A.4    Sahm, H.5
  • 8
    • 25444479070 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions
    • M. Inui, H. Kawaguchi, S. Murakami, A.A. Vertès, and H. Yukawa Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions J. Mol. Microbiol. Biotechnol. 8 2004 243 254
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.8 , pp. 243-254
    • Inui, M.1    Kawaguchi, H.2    Murakami, S.3    Vertès, A.A.4    Yukawa, H.5
  • 10
    • 77950627591 scopus 로고    scopus 로고
    • Xylitol production by recombinant Corynebacterium glutamicum under oxygen deprivation
    • M. Sasaki, T. Jojima, M. Inui, and H. Yukawa Xylitol production by recombinant Corynebacterium glutamicum under oxygen deprivation Appl. Microbiol. Biotechnol. 86 2010 1057 1066
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1057-1066
    • Sasaki, M.1    Jojima, T.2    Inui, M.3    Yukawa, H.4
  • 11
    • 56349093759 scopus 로고    scopus 로고
    • An efficient succinic acid production process in a metabolically engineered Corynebacterium glutamicum strain
    • S. Okino, R. Noburyu, M. Suda, T. Jojima, M. Inui, and H. Yukawa An efficient succinic acid production process in a metabolically engineered Corynebacterium glutamicum strain Appl. Microbiol. Biotechnol. 81 2008 459 464
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 459-464
    • Okino, S.1    Noburyu, R.2    Suda, M.3    Jojima, T.4    Inui, M.5    Yukawa, H.6
  • 12
    • 77952889404 scopus 로고    scopus 로고
    • Engineering of sugar metabolism of Corynebacterium glutamicum for production of amino acid l-alanine under oxygen deprivation
    • T. Jojima, M. Fujii, E. Mori, M. Inui, and H. Yukawa Engineering of sugar metabolism of Corynebacterium glutamicum for production of amino acid l-alanine under oxygen deprivation Appl. Microbiol. Biotechnol. 87 2010 159 165
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 159-165
    • Jojima, T.1    Fujii, M.2    Mori, E.3    Inui, M.4    Yukawa, H.5
  • 13
    • 80052627582 scopus 로고    scopus 로고
    • Bio-based production of the platform chemical 1,5-diaminopentane
    • S. Kind, and C. Wittmann Bio-based production of the platform chemical 1,5-diaminopentane Appl. Microbiol. Biotechnol. 91 2011 1287 1296
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 1287-1296
    • Kind, S.1    Wittmann, C.2
  • 14
    • 0347761177 scopus 로고    scopus 로고
    • Comparative metabolic flux analysis of lysine-producing Corynebacterium glutamicum cultured on glucose or fructose
    • P. Kiefer, E. Heinzle, O. Zelder, and C. Wittmann Comparative metabolic flux analysis of lysine-producing Corynebacterium glutamicum cultured on glucose or fructose Appl. Environ. Microbiol. 70 2004 229 239
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 229-239
    • Kiefer, P.1    Heinzle, E.2    Zelder, O.3    Wittmann, C.4
  • 16
    • 3042731363 scopus 로고    scopus 로고
    • Metabolic network analysis of lysine producing Corynebacterium glutamicum at a miniaturized scale
    • C. Wittmann, H.M. Kim, and E. Heinzle Metabolic network analysis of lysine producing Corynebacterium glutamicum at a miniaturized scale Biotechnol. Bioeng. 87 2004 1 6
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 1-6
    • Wittmann, C.1    Kim, H.M.2    Heinzle, E.3
  • 17
    • 77955956714 scopus 로고    scopus 로고
    • Regulation of the expression of genes involved in NAD de novo biosynthesis in Corynebacterium glutamicum
    • H. Teramoto, M. Suda, M. Inui, and H. Yukawa Regulation of the expression of genes involved in NAD de novo biosynthesis in Corynebacterium glutamicum Appl. Environ. Microbiol. 76 2010 5488 5495
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5488-5495
    • Teramoto, H.1    Suda, M.2    Inui, M.3    Yukawa, H.4
  • 18
    • 84856138130 scopus 로고    scopus 로고
    • Improvement of the redox balance increases l-valine production by Corynebacterium glutamicum under oxygen deprivation
    • S. Hasegawa, K. Uematsu, Y. Natsuma, M. Suda, K. Hiraga, T. Jojima, M. Inui, and H. Yukawa Improvement of the redox balance increases l-valine production by Corynebacterium glutamicum under oxygen deprivation Appl. Environ. Microbiol. 78 2011 865 875
    • (2011) Appl. Environ. Microbiol. , vol.78 , pp. 865-875
    • Hasegawa, S.1    Uematsu, K.2    Natsuma, Y.3    Suda, M.4    Hiraga, K.5    Jojima, T.6    Inui, M.7    Yukawa, H.8
  • 19
    • 73349135662 scopus 로고    scopus 로고
    • Engineering of pentose transport in Corynebacterium glutamicum to improve simultaneous utilization of mixed sugars
    • M. Sasaki, T. Jojima, H. Kawaguchi, M. Inui, and H. Yukawa Engineering of pentose transport in Corynebacterium glutamicum to improve simultaneous utilization of mixed sugars Appl. Microbiol. Biotechnol. 85 2009 105 115
    • (2009) Appl. Microbiol. Biotechnol. , vol.85 , pp. 105-115
    • Sasaki, M.1    Jojima, T.2    Kawaguchi, H.3    Inui, M.4    Yukawa, H.5
  • 20
    • 1642268980 scopus 로고    scopus 로고
    • Microtiter assay for glutamine synthetase biosynthetic activity using inorganic phosphate detection
    • J.D. Gawronski, and D.R. Benson Microtiter assay for glutamine synthetase biosynthetic activity using inorganic phosphate detection Anal. Biochem. 327 2004 114 118
    • (2004) Anal. Biochem. , vol.327 , pp. 114-118
    • Gawronski, J.D.1    Benson, D.R.2
  • 21
    • 79955755634 scopus 로고    scopus 로고
    • Determination of dihydroxyacetone and glycerol in fermentation process by GC after n-methylimidazole catalyzed acetylation
    • J. Wu, M.H. Li, J.P. Lin, and D.Z. Wei Determination of dihydroxyacetone and glycerol in fermentation process by GC after n-methylimidazole catalyzed acetylation J. Chromatogr. Sci. 49 2011 375 378
    • (2011) J. Chromatogr. Sci. , vol.49 , pp. 375-378
    • Wu, J.1    Li, M.H.2    Lin, J.P.3    Wei, D.Z.4
  • 22
    • 33646594074 scopus 로고    scopus 로고
    • High-throughput transposon mutagenesis of Corynebacterium glutamicum and construction of a single-gene disruptant mutant library
    • N. Suzuki, N. Okai, H. Nonaka, Y. Tsuge, M. Inui, and H. Yukawa High-throughput transposon mutagenesis of Corynebacterium glutamicum and construction of a single-gene disruptant mutant library Appl. Environ. Microbiol. 72 2006 3750 3755
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3750-3755
    • Suzuki, N.1    Okai, N.2    Nonaka, H.3    Tsuge, Y.4    Inui, M.5    Yukawa, H.6
  • 23
    • 31544471658 scopus 로고    scopus 로고
    • Structure and activity analyses of Escherichia coli K-12 NagD provide insight into the evolution of biochemical function in the haloalkanoic acid dehalogenase superfamily
    • L.W. Tremblay, D. Dunaway-Mariano, and K.N. Allen Structure and activity analyses of Escherichia coli K-12 NagD provide insight into the evolution of biochemical function in the haloalkanoic acid dehalogenase superfamily Biochemistry 45 2006 1183 1193
    • (2006) Biochemistry , vol.45 , pp. 1183-1193
    • Tremblay, L.W.1    Dunaway-Mariano, D.2    Allen, K.N.3
  • 26
    • 10444258178 scopus 로고    scopus 로고
    • Metabolic fluxes in Corynebacterium glutamicum during lysine production with sucrose as carbon source
    • C. Wittmann, P. Kiefer, and O. Zelder Metabolic fluxes in Corynebacterium glutamicum during lysine production with sucrose as carbon source Appl. Environ. Microbiol. 70 2004 7277 7287
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 7277-7287
    • Wittmann, C.1    Kiefer, P.2    Zelder, O.3
  • 27
    • 1542376957 scopus 로고    scopus 로고
    • In-depth profiling of lysine-producing Corynebacterium glutamicum by combined analysis of the transcriptome, metabolome, and fluxome
    • J.O. Krömer, O. Sorgenfrei, K. Klopprogge, E. Heinzle, and C. Wittmann In-depth profiling of lysine-producing Corynebacterium glutamicum by combined analysis of the transcriptome, metabolome, and fluxome J. Bacteriol. 186 2004 1769 1784
    • (2004) J. Bacteriol. , vol.186 , pp. 1769-1784
    • Krömer, J.O.1    Sorgenfrei, O.2    Klopprogge, K.3    Heinzle, E.4    Wittmann, C.5
  • 28
    • 42449109972 scopus 로고    scopus 로고
    • Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum
    • J. Becker, C. Klopprogge, and C. Wittmann Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum Microb. Cell Fact. 7 2008 8
    • (2008) Microb. Cell Fact. , vol.7 , pp. 8
    • Becker, J.1    Klopprogge, C.2    Wittmann, C.3
  • 29
    • 27744506402 scopus 로고    scopus 로고
    • Amplified expression of fructose 1,6-bisphosphatase in Corynebacterium glutamicum increases in vivo flux through the pentose phosphate pathway and lysine production on different carbon sources
    • J. Becker, C. Klopprogge, O. Zelder, E. Heinzle, and C. Wittmann Amplified expression of fructose 1,6-bisphosphatase in Corynebacterium glutamicum increases in vivo flux through the pentose phosphate pathway and lysine production on different carbon sources Appl. Environ. Microbiol. 71 2005 8587 8596
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8587-8596
    • Becker, J.1    Klopprogge, C.2    Zelder, O.3    Heinzle, E.4    Wittmann, C.5
  • 30
    • 33746922036 scopus 로고    scopus 로고
    • Evolutionary genomics of the HAD superfamily: Understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes
    • A.M. Burroughs, K.N. Allen, D. Dunaway-Mariano, and L. Aravind Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes J. Mol. Biol. 361 2006 1003 1034
    • (2006) J. Mol. Biol. , vol.361 , pp. 1003-1034
    • Burroughs, A.M.1    Allen, K.N.2    Dunaway-Mariano, D.3    Aravind, L.4
  • 32
    • 79959967962 scopus 로고    scopus 로고
    • Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis
    • L.M. Godinho, and I. de Sa-Nogueira Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis FEBS J. 278 2011 2511 2524
    • (2011) FEBS J. , vol.278 , pp. 2511-2524
    • Godinho, L.M.1    De Sa-Nogueira, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.