메뉴 건너뛰기




Volumn 41, Issue 6, 2007, Pages 962-973

Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes

Author keywords

glucosidase; Domain structure; Enzyme classification; Gene annotation; Gene duplication; GH31 family; Glycoside hydrolase; Multiple sequence alignment; Paralog; Protein family; Protein phylogenetic tree; Starch utilization

Indexed keywords

CHORDATA; MAMMALIA;

EID: 37349047777     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893307060131     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane orientation, and evolution of a stalked, intrinsic brush border protein
    • Hunziker W., Spiess M., Semenza G., Lodish H.F. 1986. The sucrase-isomaltase complex: Primary structure, membrane orientation, and evolution of a stalked, intrinsic brush border protein. Cell. 46, 227-234.
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 2
    • 0032579520 scopus 로고    scopus 로고
    • Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase
    • Nichols B.L., Eldering J., Avery S., Hahn D., Quaroni A., Sterchi E. 1998. Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J. Biol. Chem. 273, 3076-3081.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3076-3081
    • Nichols, B.L.1    Eldering, J.2    Avery, S.3    Hahn, D.4    Quaroni, A.5    Sterchi, E.6
  • 3
    • 0037417990 scopus 로고    scopus 로고
    • The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities
    • Nichols B.L., Avery S., Sen P., Swallow D.M., Hahn D., Sterchi E. 2003. The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities. Proc. Natl. Acad. Sci. USA. 100, 1432-1437.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 1432-1437
    • Nichols, B.L.1    Avery, S.2    Sen, P.3    Swallow, D.M.4    Hahn, D.5    Sterchi, E.6
  • 4
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 6
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
    • Lovering A.L., Lee S.S., Kim Y.W., Withers S.G., Strynadka N.C. 2005. Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem. 280, 2105-2115.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.W.3    Withers, S.G.4    Strynadka, N.C.5
  • 7
    • 33745048293 scopus 로고    scopus 로고
    • Structure of the Sulfolobus solfataricus α-glucosidase: Implications for domain conservation and substrate recognition in GH31
    • Ernst H.A., Leggio L.L., Willemoes M., Leonard G., Blum P., Larsen S. 2006. Structure of the Sulfolobus solfataricus α-glucosidase: Implications for domain conservation and substrate recognition in GH31. J. Mol. Biol. 358, 1106-1124.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1106-1124
    • Ernst, H.A.1    Leggio, L.L.2    Willemoes, M.3    Leonard, G.4    Blum, P.5    Larsen, S.6
  • 8
    • 3042749528 scopus 로고    scopus 로고
    • Sequence analysis of glycosylhydrolases: β-fructosidase and α-galactosidase superfamilies
    • Naumoff D.G. 2001. Sequence analysis of glycosylhydrolases: β-fructosidase and α-galactosidase superfamilies. Glycoconjugate J. 18, 109.
    • (2001) Glycoconjugate J. , vol.18 , pp. 109
    • Naumoff, D.G.1
  • 10
    • 0037125202 scopus 로고    scopus 로고
    • Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13
    • Rigden D.J. 2002. Iterative database searches demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13. FEBS Lett. 523, 17-22.
    • (2002) FEBS Lett. , vol.523 , pp. 17-22
    • Rigden, D.J.1
  • 11
    • 3042747192 scopus 로고    scopus 로고
    • α-Galactosidase superfamily: Phylogenetic analysis and homology with some α-glucosidases
    • Groningen, the Netherlands
    • Naumoff D.G. 2003. α-Galactosidase superfamily: Phylogenetic analysis and homology with some α-glucosidases. Program and Abstracts of the 5th Carbohydrate Bioengineering Meeting, Groningen, the Netherlands, p. 81.
    • (2003) Program and Abstracts of the 5th Carbohydrate Bioengineering Meeting , pp. 81
    • Naumoff, D.G.1
  • 12
    • 6944235310 scopus 로고    scopus 로고
    • Phylogenetic analysis of α-galactosodases of the GH27 family
    • Naumoff D.G. 2004. Phylogenetic analysis of α-galactosodases of the GH27 family. Mol. Biol. 38, 463-467.
    • (2004) Mol. Biol. , vol.38 , pp. 463-467
    • Naumoff, D.G.1
  • 13
    • 25444457045 scopus 로고    scopus 로고
    • The α-galactosidase superfamily: Sequence based classification of α-galactosidases and related glycosidases
    • July 25-30, 2004
    • Naumoff D.G. 2004. The α-galactosidase superfamily: Sequence based classification of α-galactosidases and related glycosidases. Proc. Fourth Int. Conf. on Bioinformatics of Genome Regulation and Structure, July 25-30, 2004, Novosibirsk, Russia, vol. 1, pp. 315-318 ( http://www.bionet.nsc.ru/ meeting/bgrs2004/tom1.pdf ).
    • (2004) Proc. Fourth Int. Conf. on Bioinformatics of Genome Regulation and Structure , vol.1 , pp. 315-318
    • Naumoff, D.G.1
  • 14
    • 37349126042 scopus 로고    scopus 로고
    • Development of a hierarchical classification of the TIM-barrel type glycoside hydrolases
    • July 16-22, 2006, Novosibirsk, Russia
    • Naumoff D.G. 2006. Development of a hierarchical classification of the TIM-barrel type glycoside hydrolases. Proc. Fifth Int. Conf. on Bioinformatics of Genome Regulation and Structure, July 16-22, 2006, Novosibirsk, Russia, vol. 1, pp. 294-298 ( http://www.bionet. nsc.ru/meeting/bgrs2006/BGRS_2006_V1.pdf ).
    • (2006) Proc. Fifth Int. Conf. on Bioinformatics of Genome Regulation and Structure , vol.1 , pp. 294-298
    • Naumoff, D.G.1
  • 15
    • 0029915713 scopus 로고    scopus 로고
    • Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides
    • McCarter J.D., Withers S.G. 1996. Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides. J. Biol. Chem. 271, 6889-6894.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6889-6894
    • McCarter, J.D.1    Withers, S.G.2
  • 16
    • 0032059448 scopus 로고    scopus 로고
    • Glycosidase families
    • Henrissat B. 1998. Glycosidase families. Biochem. Soc. Trans. 26, 153-156.
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 17
    • 33748706708 scopus 로고    scopus 로고
    • Probing the structure of glucan lyases by sequence analysis, circular dichroism and proteolysis
    • Ernst H.A., Leggio L.L., Yu S., Finnie C., Svensson B., Larsen S. 2005. Probing the structure of glucan lyases by sequence analysis, circular dichroism and proteolysis. Biologia (Bratislava). 60, 149-159.
    • (2005) Biologia (Bratislava) , vol.60 , pp. 149-159
    • Ernst, H.A.1    Leggio, L.L.2    Yu, S.3    Finnie, C.4    Svensson, B.5    Larsen, S.6
  • 18
    • 25444464874 scopus 로고    scopus 로고
    • GH97 is a new family of glycoside hydrolases, which is related to the α-galactosidase superfamily
    • Art. 112.
    • Naumoff D.G. 2005. GH97 is a new family of glycoside hydrolases, which is related to the α-galactosidase superfamily. BMC Genomics. 6, Art. 112.
    • (2005) BMC Genomics , vol.6
    • Naumoff, D.G.1
  • 19
    • 33947530379 scopus 로고    scopus 로고
    • A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31
    • Janeȩk Š., Svensson B., Macgregor E.A. 2007. A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31. FEBS Lett. 581, 1261-1268.
    • (2007) FEBS Lett. , vol.581 , pp. 1261-1268
    • Janeȩk1    Svensson, B.2    MacGregor, E.A.3
  • 20
    • 37349105441 scopus 로고    scopus 로고
    • Gene structure and evolution of mammalian maltase-glucoamylase
    • July 23-28, 2006, Whistler, Canada Abstr. THU-C4-AM.1.
    • Naumoff D.G. 2006. Gene structure and evolution of mammalian maltase-glucoamylase. Abstr. XXIII Int. Carbohydrate Symposium, July 23-28, 2006, Whistler, Canada, p. 244. Abstr. THU-C4-AM.1.
    • (2006) Abstr. XXIII Int. Carbohydrate Symposium , pp. 244
    • Naumoff, D.G.1
  • 21
    • 0035234086 scopus 로고    scopus 로고
    • Molecular structure of the Lactobacillus plantarum sucrose utilization locus: Comparison with Pediococcus pentosaceus
    • Naumoff D.G., Livshits V.A. 2001. Molecular structure of the Lactobacillus plantarum sucrose utilization locus: Comparison with Pediococcus pentosaceus. Mol. Biol. 35, 19-27.
    • (2001) Mol. Biol. , vol.35 , pp. 19-27
    • Naumoff, D.G.1    Livshits, V.A.2
  • 22
    • 0035177354 scopus 로고    scopus 로고
    • β-Fructosidase superfamily: Homology with some β-L-arabinases and β-D-xylosidases
    • Naumoff D.G. 2001. β-Fructosidase superfamily: Homology with some β-L-arabinases and β-D-xylosidases. Prot. Struct. Funct. Genet. 42, 66-76.
    • (2001) Prot. Struct. Funct. Genet. , vol.42 , pp. 66-76
    • Naumoff, D.G.1
  • 23
    • 37349050394 scopus 로고    scopus 로고
    • Phylogenetic analysis of COG1649, a new family of predicted glycosyl hydrolases
    • July 16-22, 2006, Novosibirsk, Russia
    • Kuznetsova A.Y., Naumoff D.G. 2006. Phylogenetic analysis of COG1649, a new family of predicted glycosyl hydrolases. Proc. Fifth Int. Conf. on Bioinformatics of Genome Regulation and Structure, July 16-22, 2006, Novosibirsk, Russia, vol. 3, pp. 179-182 ( http://www.bionet.nsc.ru/meeting/ bgrs2006/BGRS_2006_V3.pdf ).
    • (2006) Proc. Fifth Int. Conf. on Bioinformatics of Genome Regulation and Structure , vol.3 , pp. 179-182
    • Kuznetsova, A.Y.1    Naumoff, D.G.2
  • 24
    • 37349081352 scopus 로고    scopus 로고
    • Phylogenetic analysis of a protein family
    • Art. 3
    • Naumoff D.G. 2006. Phylogenetic analysis of a protein family. Zbio. 1, Art. 3 ( http://zbio.net/bio/001/003.html ).
    • (2006) Zbio. , vol.1
    • Naumoff, D.G.1
  • 25
    • 0032921044 scopus 로고    scopus 로고
    • The Neocallimastix patriciarum cellulase, CelD, contains three almost identical catalytic domains with high specific activities on Avicel
    • Aylward J.H., Gobius K.S., Xue G.-P., Simpson G.D., Dalrymple B.P. 1999. The Neocallimastix patriciarum cellulase, CelD, contains three almost identical catalytic domains with high specific activities on Avicel. Enzyme Microb. Technol. 24, 609-614.
    • (1999) Enzyme Microb. Technol. , vol.24 , pp. 609-614
    • Aylward, J.H.1    Gobius, K.S.2    Xue, G.-P.3    Simpson, G.D.4    Dalrymple, B.P.5
  • 26
    • 0033871139 scopus 로고    scopus 로고
    • Primary sequence and enzymic properties of two modular endoglucanases, Cel5A and Cel45A, from the anaerobic fungus Piromyces equi
    • Eberhardt R.Y., Gilbert H.J., Hazlewood G.P. 2000. Primary sequence and enzymic properties of two modular endoglucanases, Cel5A and Cel45A, from the anaerobic fungus Piromyces equi. Microbiology. 146, 1999-2008.
    • (2000) Microbiology , vol.146 , pp. 1999-2008
    • Eberhardt, R.Y.1    Gilbert, H.J.2    Hazlewood, G.P.3
  • 27
    • 26844496302 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of a Eubacterium cellulosolvens 5 gene encoding an endoglucanase (Cel5A) with novel carbohydrate-binding modules, and properties of Cel5A
    • Yoda K., Toyoda A., Mukoyama Y., Nakamura Y., Minato H. 2005. Cloning, sequencing, and expression of a Eubacterium cellulosolvens 5 gene encoding an endoglucanase (Cel5A) with novel carbohydrate-binding modules, and properties of Cel5A. Appl. Environ. Microbiol. 71, 5787-5793.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5787-5793
    • Yoda, K.1    Toyoda, A.2    Mukoyama, Y.3    Nakamura, Y.4    Minato, H.5
  • 28
    • 0029661443 scopus 로고    scopus 로고
    • Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites
    • Hatada Y., Igarashi K., Ozaki K., Ara K., Hitomi J., Kobayashi T., Kawai S., Watabe T., Ito S. 1996. Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites. J. Biol. Chem. 271, 24,075-24,083.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24
    • Hatada, Y.1    Igarashi, K.2    Ozaki, K.3    Ara, K.4    Hitomi, J.5    Kobayashi, T.6    Kawai, S.7    Watabe, T.8    Ito, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.