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Volumn 589, Issue 10, 2015, Pages 1089-1094

Vibrio vulnificus glycogen branching enzyme preferentially transfers very short chains: N1 domain determines the chain length transferred

Author keywords

Branching pattern; Domain manipulated mutant; Glycogen branching enzymes (GBE); N terminal domain; Vibrio vulnificus

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; BACTERIAL PROTEIN; GLYCOGEN; HYBRID PROTEIN;

EID: 84933519304     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.03.011     Document Type: Article
Times cited : (40)

References (32)
  • 1
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • P.J. Roach Glycogen and its metabolism Curr. Mol. Med. 2 2002 101 120
    • (2002) Curr. Mol. Med. , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 2
    • 0035161939 scopus 로고    scopus 로고
    • Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae
    • J. François, and J.L. Parrou Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae FEMS Microbiol. Rev. 25 2001 125 145
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 125-145
    • François, J.1    Parrou, J.L.2
  • 4
    • 0017404313 scopus 로고
    • Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan: α-1,4-glucan 6-glycosyltransferase
    • C. Boyer, and J. Preiss Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan: α-1,4-glucan 6-glycosyltransferase Biochemistry 16 1977 3693 3699
    • (1977) Biochemistry , vol.16 , pp. 3693-3699
    • Boyer, C.1    Preiss, J.2
  • 5
    • 84899863334 scopus 로고    scopus 로고
    • α-Amylase: An enzyme specificity found in various families of glycoside hydrolases
    • Š. Janeček, B. Svensson, and E.A. MacGregor α-Amylase: an enzyme specificity found in various families of glycoside hydrolases Cell. Mol. Life Sci. 71 2014 1149 1170
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 1149-1170
    • Janeček, S.1    Svensson, B.2    Macgregor, E.A.3
  • 6
    • 78650791313 scopus 로고    scopus 로고
    • Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1
    • C.R. Santos, C.C. Tonoli, D.M. Trindade, C. Betzel, H. Takata, T. Kuriki, T. Kanai, T. Imanaka, R.K. Arni, and M.T. Murakami Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1 Proteins: Struct. Funct. Bioinform. 79 2011 547 557
    • (2011) Proteins: Struct. Funct. Bioinform. , vol.79 , pp. 547-557
    • Santos, C.R.1    Tonoli, C.C.2    Trindade, D.M.3    Betzel, C.4    Takata, H.5    Kuriki, T.6    Kanai, T.7    Imanaka, T.8    Arni, R.K.9    Murakami, M.T.10
  • 8
    • 61649113784 scopus 로고    scopus 로고
    • The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains
    • M. Palomo, S. Kralj, M. van der Maarel, and L. Dijkhuizen The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains Appl. Environ. Microbiol. 75 2009 1355 1362
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1355-1362
    • Palomo, M.1    Kralj, S.2    Van Der Maarel, M.3    Dijkhuizen, L.4
  • 9
    • 0031172327 scopus 로고    scopus 로고
    • Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme
    • H. Guan, P. Li, J. Imparl-Radosevich, J. Preiss, and P. Keeling Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme Arch. Biochem. Biophys. 342 1997 92 98
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 92-98
    • Guan, H.1    Li, P.2    Imparl-Radosevich, J.3    Preiss, J.4    Keeling, P.5
  • 10
    • 0027991845 scopus 로고
    • Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus
    • H. Takata, T. Takaha, T. Kuriki, S. Okada, M. Takagi, and T. Imanaka Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus Appl. Environ. Microbiol. 60 1994 3096 3104
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3096-3104
    • Takata, H.1    Takaha, T.2    Kuriki, T.3    Okada, S.4    Takagi, M.5    Imanaka, T.6
  • 13
    • 84863239712 scopus 로고    scopus 로고
    • Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus
    • T.Y. Jung, D. Li, J.T. Park, S.M. Yoon, P.L. Tran, B.H. Oh, Š. Janeček, S.G. Park, E.J. Woo, and K.H. Park Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus J. Biol. Chem. 287 2012 7979 7989
    • (2012) J. Biol. Chem. , vol.287 , pp. 7979-7989
    • Jung, T.Y.1    Li, D.2    Park, J.T.3    Yoon, S.M.4    Tran, P.L.5    Oh, B.H.6    Janeček, S.7    Park, S.G.8    Woo, E.J.9    Park, K.H.10
  • 14
    • 0034657390 scopus 로고    scopus 로고
    • Limited proteolysis of branching enzyme from Escherichia coli
    • K. Binderup, R. Mikkelsen, and J. Preiss Limited proteolysis of branching enzyme from Escherichia coli Arch. Biochem. Biophys. 377 2000 366 371
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 366-371
    • Binderup, K.1    Mikkelsen, R.2    Preiss, J.3
  • 15
    • 57349180133 scopus 로고    scopus 로고
    • Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-binding module family 48
    • M. Machovič, and Š. Janeček Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-binding module family 48 Biologia 63 2008 1057 1068
    • (2008) Biologia , vol.63 , pp. 1057-1068
    • Machovič, M.1    Janeček, S.2
  • 16
    • 84923698079 scopus 로고    scopus 로고
    • Novel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium
    • I.N. Oh, J.L. Jane, K. Wang, J.T. Park, and K.H. Park Novel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium Extremophiles 19 2015 363 371
    • (2015) Extremophiles , vol.19 , pp. 363-371
    • Oh, I.N.1    Jane, J.L.2    Wang, K.3    Park, J.T.4    Park, K.H.5
  • 17
    • 84897060453 scopus 로고    scopus 로고
    • A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch
    • H. Peng, Y. Zheng, M. Chen, Y. Wang, Y. Xiao, and Y. Gao A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch FEBS Lett. 588 2014 1161 1167
    • (2014) FEBS Lett. , vol.588 , pp. 1161-1167
    • Peng, H.1    Zheng, Y.2    Chen, M.3    Wang, Y.4    Xiao, Y.5    Gao, Y.6
  • 18
    • 35348897943 scopus 로고    scopus 로고
    • Oligosaccharide recognition and binding to the carbohydrate binding module of AMP-activated protein kinase
    • A. Koay, K.A. Rimmer, H.D. Mertens, P.R. Gooley, and D. Stapleton Oligosaccharide recognition and binding to the carbohydrate binding module of AMP-activated protein kinase FEBS Lett. 581 2007 5055 5059
    • (2007) FEBS Lett. , vol.581 , pp. 5055-5059
    • Koay, A.1    Rimmer, K.A.2    Mertens, H.D.3    Gooley, P.R.4    Stapleton, D.5
  • 19
    • 77954240010 scopus 로고    scopus 로고
    • Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme INSIGHTS of N-TERMINAL β-SANDWICH in SUBSTRATE SPECIFICITY and ENZYMATIC ACTIVITY
    • K. Pal, S. Kumar, S. Sharma, S.K. Garg, M.S. Alam, H.E. Xu, P. Agrawal, and K. Swaminathan Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme INSIGHTS OF N-TERMINAL β-SANDWICH IN SUBSTRATE SPECIFICITY AND ENZYMATIC ACTIVITY J. Biol. Chem. 285 2010 20897 20903
    • (2010) J. Biol. Chem. , vol.285 , pp. 20897-20903
    • Pal, K.1    Kumar, S.2    Sharma, S.3    Garg, S.K.4    Alam, M.S.5    Xu, H.E.6    Agrawal, P.7    Swaminathan, K.8
  • 29
    • 80054980829 scopus 로고    scopus 로고
    • Glycogen with short average chain length enhances bacterial durability
    • L. Wang, and M.J. Wise Glycogen with short average chain length enhances bacterial durability Naturwissenschaften 98 2011 719 729
    • (2011) Naturwissenschaften , vol.98 , pp. 719-729
    • Wang, L.1    Wise, M.J.2
  • 30
    • 84946060416 scopus 로고    scopus 로고
    • SMART: Recent updates, new developments and status in 2015
    • I. Letunic, T. Doerks, and P. Bork SMART: recent updates, new developments and status in 2015 Nucleic Acids Res. 43 2015 D257 D260
    • (2015) Nucleic Acids Res. , vol.43 , pp. D257-D260
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 31
    • 0037082135 scopus 로고    scopus 로고
    • Truncation of the amino terminus of branching enzyme changes its chain transfer pattern
    • K. Binderup, R. Mikkelsen, and J. Preiss Truncation of the amino terminus of branching enzyme changes its chain transfer pattern Arch. Biochem. Biophys. 397 2002 279 285
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 279-285
    • Binderup, K.1    Mikkelsen, R.2    Preiss, J.3
  • 32
    • 0141567087 scopus 로고    scopus 로고
    • Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus
    • C.H. Devillers, M.E. Piper, M.A. Ballicora, and J. Preiss Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus Arch. Biochem. Biophys. 418 2003 34 38
    • (2003) Arch. Biochem. Biophys. , vol.418 , pp. 34-38
    • Devillers, C.H.1    Piper, M.E.2    Ballicora, M.A.3    Preiss, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.