메뉴 건너뛰기




Volumn 386, Issue 2, 2005, Pages 227-236

Human xylosyltransferase I: Functional and biochemical characterization of cysteine residues required for enzymic activity

Author keywords

Cysteine; Functional characterization; Glycosaminoglycan; Proteoglycan; Site directed mutagenesis; Xylosyltransferase I

Indexed keywords

BINDING ENERGY; BIOSYNTHESIS; CATALYSIS; CELLS; DIMERS; ELECTROPHORESIS; MUTAGENESIS;

EID: 14844298775     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041206     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen, L. and Lindahl, U. (1991) Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60, 443-475
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 2
    • 0023049693 scopus 로고
    • Proteoglycans in health and disease: Structures and functions
    • Poole, A. R. (1986) Proteoglycans in health and disease: structures and functions. Biochem. J. 236, 1-14
    • (1986) Biochem. J. , vol.236 , pp. 1-14
    • Poole, A.R.1
  • 3
    • 0024402592 scopus 로고
    • Proteoglycans in cell regulation
    • Ruoslahti, E. (1989) Proteoglycans in cell regulation. J. Biol. Chem. 264, 13369-13372
    • (1989) J. Biol. Chem. , vol.264 , pp. 13369-13372
    • Ruoslahti, E.1
  • 4
    • 0029795565 scopus 로고    scopus 로고
    • Heparan sulfate: A piece of information
    • Salmivirta, M., Lidholt, K. and Lindahl, U. (1996) Heparan sulfate: a piece of information. FASEB J. 10, 1270-1279
    • (1996) FASEB J. , vol.10 , pp. 1270-1279
    • Salmivirta, M.1    Lidholt, K.2    Lindahl, U.3
  • 5
    • 0033613948 scopus 로고    scopus 로고
    • Molecular cloning and expression of a third member of the heparansulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase family
    • Aikawa, J. and Esko, J. D. (1999) Molecular cloning and expression of a third member of the heparansulfate/heparin GlcNAc N-deacetylase/N- sulfotransferase family. J. Biol. Chem. 274, 2690-2695
    • (1999) J. Biol. Chem. , vol.274 , pp. 2690-2695
    • Aikawa, J.1    Esko, J.D.2
  • 7
    • 0009674358 scopus 로고
    • Age-related changes in the structure of the proteoglycan subunits form human articular cartilage
    • Roughley, P. J. and White, R. J. (1980) Age-related changes in the structure of the proteoglycan subunits form human articular cartilage. J. Biol. Chem. 264, 13369-13372
    • (1980) J. Biol. Chem. , vol.264 , pp. 13369-13372
    • Roughley, P.J.1    White, R.J.2
  • 8
    • 0031465169 scopus 로고    scopus 로고
    • Developmental regulation of the sulfation profile of chondroitin sulfate chain in the chicken embryo brain
    • Kitagawa, H., Tsutsumi, K., Tone, Y. and Sugahara, K. (1997) Developmental regulation of the sulfation profile of chondroitin sulfate chain in the chicken embryo brain. J. Biol. Chem. 272, 31377-31381
    • (1997) J. Biol. Chem. , vol.272 , pp. 31377-31381
    • Kitagawa, H.1    Tsutsumi, K.2    Tone, Y.3    Sugahara, K.4
  • 9
    • 0001784863 scopus 로고
    • Carbohydrate-peptide linkages in proteoglycans of animal, plant and bacterial origin
    • (Gottschalk, A., ed.), Elsevier, New York
    • Lindahl, U. and Rodén, L. (1972) Carbohydrate-peptide linkages in proteoglycans of animal, plant and bacterial origin. In Glycoproteins (Gottschalk, A., ed.), pp. 491-517, Elsevier, New York
    • (1972) Glycoproteins , pp. 491-517
    • Lindahl, U.1    Rodén, L.2
  • 10
    • 0000216230 scopus 로고
    • Structure and metabolism of connective tissue proteoglycans
    • (Lennarz, W. J., ed.), Plenum, New York
    • Rodén, L. (1980) Structure and metabolism of connective tissue proteoglycans, The Biochemistry of Glycoproteins and Proteoglycans (Lennarz, W. J., ed.), pp. 269-314 Plenum, New York
    • (1980) The Biochemistry of Glycoproteins and Proteoglycans , pp. 269-314
    • Rodén, L.1
  • 11
    • 0017746397 scopus 로고
    • Regulation of chondrotin sulfate synthesis. Effect of β-xylosides on synthesis of chondroitin sulfate proteoglycan, chondrotin sulfate chains, and core protein
    • Schwartz, N. B. (1977) Regulation of chondrotin sulfate synthesis. Effect of β-xylosides on synthesis of chondroitin sulfate proteoglycan, chondrotin sulfate chains, and core protein. J. Biol. Chem. 252, 6316-6321
    • (1977) J. Biol. Chem. , vol.252 , pp. 6316-6321
    • Schwartz, N.B.1
  • 12
    • 0025719930 scopus 로고
    • Initiation of chondroitin sulfate biosynthesis: A kinetic analysis of UDP-D-xylose:core protein β-D-xylosyltransferase
    • Kearns, A. E., Campbell, S. C., Westley, J. and Schwartz, N. B. (1991) Initiation of chondroitin sulfate biosynthesis: a kinetic analysis of UDP-D-xylose:core protein β-D-xylosyltransferase. Biochemestry 30, 7477-7483
    • (1991) Biochemestry , vol.30 , pp. 7477-7483
    • Kearns, A.E.1    Campbell, S.C.2    Westley, J.3    Schwartz, N.B.4
  • 13
    • 0021323991 scopus 로고
    • Location of xylosyltransferase in the cisternae of the rough endoplasmic reticulum of embryonic chick cartilage cells
    • Hoffmann, H. P., Schwartz, N. B., Roden, L. and Prockop, D. J. (1984) Location of xylosyltransferase in the cisternae of the rough endoplasmic reticulum of embryonic chick cartilage cells. Connect. Tissue Res. 12, 151-164
    • (1984) Connect. Tissue Res. , vol.12 , pp. 151-164
    • Hoffmann, H.P.1    Schwartz, N.B.2    Roden, L.3    Prockop, D.J.4
  • 14
    • 0001186480 scopus 로고
    • Simultaneous secretion of xylosyltransferase and chondroitin sulphate proteoclycan in chondrocyte culture
    • Kahnert, H., Paddenberg, R. and Kleesiek, K. (1991) Simultaneous secretion of xylosyltransferase and chondroitin sulphate proteoclycan in chondrocyte culture. Eur. J. Clin. Chem. Clin. Biochem. 29, 624-625
    • (1991) Eur. J. Clin. Chem. Clin. Biochem. , vol.29 , pp. 624-625
    • Kahnert, H.1    Paddenberg, R.2    Kleesiek, K.3
  • 16
    • 2442602100 scopus 로고    scopus 로고
    • The never-ending story of peptide O-xylosyltransferase
    • Wilson, I. B. H. (2004) The never-ending story of peptide O-xylosyltransferase. Cell. Mol. Life Sci. 61, 794-809
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 794-809
    • Wilson, I.B.H.1
  • 17
    • 0034624041 scopus 로고    scopus 로고
    • Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II
    • Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. (2000) Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304, 517-528
    • (2000) J. Mol. Biol. , vol.304 , pp. 517-528
    • Götting, C.1    Kuhn, J.2    Zahn, R.3    Brinkmann, T.4    Kleesiek, K.5
  • 18
    • 0037077267 scopus 로고    scopus 로고
    • Functional characterisation of Drosophila melanogaster peptide O-xylosyltransferase, the key enzyme for proteoglycan chain initiation and member of the core 2/I N-acetylglucosaminyltransferase family
    • Wilson, I. B. (2002) Functional characterisation of Drosophila melanogaster peptide O-xylosyltransferase, the key enzyme for proteoglycan chain initiation and member of the core 2/I N-acetylglucosaminyltransferase family. J. Biol. Chem. 277, 21207-21212
    • (2002) J. Biol. Chem. , vol.277 , pp. 21207-21212
    • Wilson, I.B.1
  • 19
    • 0038413758 scopus 로고    scopus 로고
    • The Caenorhabidits elegans genes sqv-2 and sqv-6, which are required for vulval morphogenesis, encode glydosaminoglycan galactosyltransferase II and xylosyltransferase
    • Hwang, H. Y., Olson, S. K., Brown, J. R., Esko, J. D. and Horvitz, H. R. (2003) The Caenorhabidits elegans genes sqv-2 and sqv-6, which are required for vulval morphogenesis, encode glydosaminoglycan galactosyltransferase II and xylosyltransferase. J. Biol. Chem. 278, 11735-11738
    • (2003) J. Biol. Chem. , vol.278 , pp. 11735-11738
    • Hwang, H.Y.1    Olson, S.K.2    Brown, J.R.3    Esko, J.D.4    Horvitz, H.R.5
  • 20
    • 0034637438 scopus 로고    scopus 로고
    • Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites
    • Holmes, E. H., Yen, T. Y. Thomas, S., Josh, R., Nguyen, A., Long, T., Gallet, F., Maftah, A., Julien, R. and Macher, B. (2000) Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites. J. Biol. Chem. 275, 24237-24245
    • (2000) J. Biol. Chem. , vol.275 , pp. 24237-24245
    • Holmes, E.H.1    Yen, T.Y.2    Thomas, S.3    Josh, R.4    Nguyen, A.5    Long, T.6    Gallet, F.7    Maftah, A.8    Julien, R.9    Macher, B.10
  • 21
    • 0027522253 scopus 로고
    • Expression of deletion constructs of bovine beta-1,4- galactosyltransferase in Escherichia coli: Importance of Cys134 for its activity
    • Boeggeman, E. E., Balaji, P. V., Sethi, N., Masibay, A. S. and Quasba, P. K. (1993) Expression of deletion constructs of bovine beta-1,4- galactosyltransferase in Escherichia coli: importance of Cys134 for its activity. Protein Eng. 6, 779-785
    • (1993) Protein Eng. , vol.6 , pp. 779-785
    • Boeggeman, E.E.1    Balaji, P.V.2    Sethi, N.3    Masibay, A.S.4    Quasba, P.K.5
  • 23
    • 0035805602 scopus 로고    scopus 로고
    • Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond
    • Datta, A. K., Chammas, R. and Paulson, J. C. (2001) Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond. J. Biol. Chem. 276, 15200-15207
    • (2001) J. Biol. Chem. , vol.276 , pp. 15200-15207
    • Datta, A.K.1    Chammas, R.2    Paulson, J.C.3
  • 24
    • 0029965591 scopus 로고    scopus 로고
    • Glycosylation defect in Led Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene
    • Puthalakath, H., Burke, J. and Gleeson, P. A. (1996) Glycosylation defect in Led Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene. J. Biol. Chem. 271, 27818-27822
    • (1996) J. Biol. Chem. , vol.271 , pp. 27818-27822
    • Puthalakath, H.1    Burke, J.2    Gleeson, P.A.3
  • 25
    • 0035805605 scopus 로고    scopus 로고
    • Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity
    • Angata, K., Yen, T. Y., El-Battari, A., Macher, B. A. and Fukuda, M. (2001) Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity. J. Biol. Chem. 276, 15369-15377
    • (2001) J. Biol. Chem. , vol.276 , pp. 15369-15377
    • Angata, K.1    Yen, T.Y.2    El-Battari, A.3    Macher, B.A.4    Fukuda, M.5
  • 27
    • 0030935527 scopus 로고    scopus 로고
    • Recognition of acceptor proteins by UDP-D-xylose proteoglycan core protein β-D-xylosyltransferase
    • Brinkmann, T., Weilke, C. and Kleesiek, K. (1997) Recognition of acceptor proteins by UDP-D-xylose proteoglycan core protein β-D-xylosyltransferase. J. Biol. Chem. 272 11171-11175
    • (1997) J. Biol. Chem. , vol.272 , pp. 11171-11175
    • Brinkmann, T.1    Weilke, C.2    Kleesiek, K.3
  • 28
    • 0031012034 scopus 로고    scopus 로고
    • Determination of xylosyltransferase activity in serum with recombinant human bikunin as acceptor
    • Weilke, C., Brinkmann, T. and Kleesiek, K. (1997) Determination of xylosyltransferase activity in serum with recombinant human bikunin as acceptor. Clin. Chem. 43, 45-51
    • (1997) Clin. Chem. , vol.43 , pp. 45-51
    • Weilke, C.1    Brinkmann, T.2    Kleesiek, K.3
  • 29
    • 0031925023 scopus 로고    scopus 로고
    • Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase
    • Götting, C., Kuhn, J., Brinkmann, T. and Kleesiek, K. (1998) Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase. J. Protein Chem. 17, 295-302
    • (1998) J. Protein Chem. , vol.17 , pp. 295-302
    • Götting, C.1    Kuhn, J.2    Brinkmann, T.3    Kleesiek, K.4
  • 30
    • 0035895906 scopus 로고    scopus 로고
    • First isolation of human UDP-D-xylose: Proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells
    • Kuhn, J., Götting, C., Schnölzer, M., Kempf, T., Brinkmann, T. and Kleesiek, K. (2001) First isolation of human UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells. J. Biol. Chem. 276, 4940-4947
    • (2001) J. Biol. Chem. , vol.276 , pp. 4940-4947
    • Kuhn, J.1    Götting, C.2    Schnölzer, M.3    Kempf, T.4    Brinkmann, T.5    Kleesiek, K.6
  • 31
    • 0029871352 scopus 로고    scopus 로고
    • A disulfide-bonded dimer of the Golgi β-galactoside α2,6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose
    • Ma, J. and Colley, K. J. (1996) A disulfide-bonded dimer of the Golgi β-galactoside α2,6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose. J. Biol. Chem. 271, 7758-7766
    • (1996) J. Biol. Chem. , vol.271 , pp. 7758-7766
    • Ma, J.1    Colley, K.J.2
  • 32
    • 0035800822 scopus 로고    scopus 로고
    • Location and mechanism of α2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerisation, localisation, activity and processing
    • Qian, R., Chen, D. and Colley, K. J. (2001) Location and mechanism of α2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerisation, localisation, activity and processing. J. Biol. Chem. 276, 28641-28649
    • (2001) J. Biol. Chem. , vol.276 , pp. 28641-28649
    • Qian, R.1    Chen, D.2    Colley, K.J.3
  • 34
    • 0034623230 scopus 로고    scopus 로고
    • Structure/function of the human Galβ1,3-glucuronyltransferase, Dimerization and funtional activity are mediated by two crucial cysteine residues
    • Ouzzine, M., Gulberti, S., Netter, P., Magdalou, J. and Fournel-Gigleux, S. (2000) Structure/function of the human Galβ1,3-glucuronyltransferase, Dimerization and funtional activity are mediated by two crucial cysteine residues. J. Biol. Chem. 275, 28254-28260
    • (2000) J. Biol. Chem. , vol.275 , pp. 28254-28260
    • Ouzzine, M.1    Gulberti, S.2    Netter, P.3    Magdalou, J.4    Fournel-Gigleux, S.5
  • 35
    • 0037016738 scopus 로고    scopus 로고
    • Purification, characterization and subunit structure of rat core 1 β1,3-galactosyltransferase
    • Ju, I, Cummings, R. D. and Canfield, W. M. (2002) Purification, characterization and subunit structure of rat core 1 β1,3- galactosyltransferase. J. Biol. Chem. 277, 169-177
    • (2002) J. Biol. Chem. , vol.277 , pp. 169-177
    • Ju, I.1    Cummings, R.D.2    Canfield, W.M.3
  • 36
    • 0031043053 scopus 로고    scopus 로고
    • Studies on the inhibition of sialyl- and galactosyltransferases
    • Kleineidam, R. G., Schneller, T., Schwarz, R. T. and Schauer, R. (1997) Studies on the inhibition of sialyl- and galactosyltransferases. Glycoconj. J. 14, 57-66
    • (1997) Glycoconj. J. , vol.14 , pp. 57-66
    • Kleineidam, R.G.1    Schneller, T.2    Schwarz, R.T.3    Schauer, R.4
  • 37
    • 0035061201 scopus 로고    scopus 로고
    • Natural and synthetic inhibitors of UDP-glucuronosyltransferase
    • Grancharov, K., Naydenova, Z., Lozeva, S. and Golovinsky, E. (2001) Natural and synthetic inhibitors of UDP-glucuronosyltransferase. Pharmacol. Ther. 89, 171-186
    • (2001) Pharmacol. Ther. , vol.89 , pp. 171-186
    • Grancharov, K.1    Naydenova, Z.2    Lozeva, S.3    Golovinsky, E.4
  • 38
    • 0036924422 scopus 로고    scopus 로고
    • High xylosyltransferase activities in human follicular fluid and cultured granulosa-lutein cells
    • Gutting, C., Kuhn, J., Tinneberg, H. R., Brinkmann, T. and Kleesiek, K. (2002) High xylosyltransferase activities in human follicular fluid and cultured granulosa-lutein cells. Mol. Hum. Reprod. 12, 1079-1086
    • (2002) Mol. Hum. Reprod. , vol.12 , pp. 1079-1086
    • Gutting, C.1    Kuhn, J.2    Tinneberg, H.R.3    Brinkmann, T.4    Kleesiek, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.