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Volumn 30, Issue 1, 2011, Pages 27-33

Dimerization of human lysyl hydroxylase 3 (LH3) is mediated by the amino acids 541-547

Author keywords

Collagen biosynthesis; Dimerization; Glucosyltransferase; Hydroxylysine; Lysyl hydroxylase; Post translational modification

Indexed keywords

2 OXOGLUTARIC ACID; COMPLEMENTARY DNA; CYSTEINE; GLYCOSYLTRANSFERASE; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE;

EID: 78951470678     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2010.10.002     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 66149151749 scopus 로고    scopus 로고
    • Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2, 6-bisphosphate allosteric site of mammalian phosphofructokinase
    • Ferreras C., Hernández E.D., Martínez-Costa O.H., Aragón J.J. Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2, 6-bisphosphate allosteric site of mammalian phosphofructokinase. J. Biol. Chem. 2009, 284:9124-9131.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9124-9131
    • Ferreras, C.1    Hernández, E.D.2    Martínez-Costa, O.H.3    Aragón, J.J.4
  • 2
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 3
    • 49549094267 scopus 로고    scopus 로고
    • Structural specificity in coiled-coil interactions
    • Grigoryan G., Keating A.E. Structural specificity in coiled-coil interactions. Curr. Opin. Struct. Biol. 2008, 18:477-483.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 477-483
    • Grigoryan, G.1    Keating, A.E.2
  • 4
    • 0026507897 scopus 로고
    • Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2
    • Hautala T., Byers M.G., Eddy R.L., Shows T.B., Kivirikko K.I., Myllylä R. Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2. Genomics 1992, 13:62-69.
    • (1992) Genomics , vol.13 , pp. 62-69
    • Hautala, T.1    Byers, M.G.2    Eddy, R.L.3    Shows, T.B.4    Kivirikko, K.I.5    Myllylä, R.6
  • 5
    • 0034680898 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity
    • Heikkinen J., Risteli M., Wang C., Latvala J., Rossi M., Valtavaara M., Myllylä R. Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J. Biol. Chem. 2000, 275:36158-36163.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36158-36163
    • Heikkinen, J.1    Risteli, M.2    Wang, C.3    Latvala, J.4    Rossi, M.5    Valtavaara, M.6    Myllylä, R.7
  • 6
    • 71449127603 scopus 로고    scopus 로고
    • Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2
    • Hyry M., Lantto J., Myllyharju J. Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2. J. Biol. Chem. 2009, 284:30917-30924.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30917-30924
    • Hyry, M.1    Lantto, J.2    Myllyharju, J.3
  • 7
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 1999, 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 8
    • 0027943512 scopus 로고
    • Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum
    • Kellokumpu S., Sormunen R., Heikkinen J., Myllylä R. Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum. J. Biol. Chem. 1994, 269:30524-30529.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30524-30529
    • Kellokumpu, S.1    Sormunen, R.2    Heikkinen, J.3    Myllylä, R.4
  • 9
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola T.K. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 2006, 7:449-456.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 10
    • 0002846317 scopus 로고    scopus 로고
    • The collagen family: structure, assembly, and organization in the extracelllular matrix
    • Wiley-Liss Inc, New York, P.M. Royce, B. Steinmann (Eds.) Connective Tissue and Its Heritable Disorders
    • Kielty C.M., Grant G.A. The collagen family: structure, assembly, and organization in the extracelllular matrix. Molecular, Genetic, and Medical Aspects 2002, 159-221. Wiley-Liss Inc, New York. second ed. P.M. Royce, B. Steinmann (Eds.).
    • (2002) Molecular, Genetic, and Medical Aspects , pp. 159-221
    • Kielty, C.M.1    Grant, G.A.2
  • 11
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
    • Kivirikko K.I., Myllylä R. Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 1982, 82, Pt A:245-304.
    • (1982) Methods Enzymol. , pp. 245-304
    • Kivirikko, K.I.1    Myllylä, R.2
  • 12
    • 0015493352 scopus 로고
    • Studies on protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of ketoglutarate
    • Kivirikko K.I., Shudo K., Sakakibara S., Prockop D.J. Studies on protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of ketoglutarate. Biochemistry 1972, 11:122-129.
    • (1972) Biochemistry , vol.11 , pp. 122-129
    • Kivirikko, K.I.1    Shudo, K.2    Sakakibara, S.3    Prockop, D.J.4
  • 13
    • 33847206745 scopus 로고    scopus 로고
    • Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity
    • Lee S., Faux C., Nixon J., Alete D., Chilton J., Hawadle M., Stoker A.W. Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity. Mol. Cell. Biol. 2007, 27:1795-1808.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1795-1808
    • Lee, S.1    Faux, C.2    Nixon, J.3    Alete, D.4    Chilton, J.5    Hawadle, M.6    Stoker, A.W.7
  • 14
    • 0037306106 scopus 로고    scopus 로고
    • Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization
    • Majumder R., Wang J., Lentz B.R. Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization. Biophys. J. 2003, 84:1238-1251.
    • (2003) Biophys. J. , vol.84 , pp. 1238-1251
    • Majumder, R.1    Wang, J.2    Lentz, B.R.3
  • 16
    • 0038106229 scopus 로고    scopus 로고
    • Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms
    • Mercer D.K., Nicol P.F., Kimbembe C., Robins S.P. Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms. Biochem. Biophys. Res. Commun. 2003, 307:803-809.
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 803-809
    • Mercer, D.K.1    Nicol, P.F.2    Kimbembe, C.3    Robins, S.P.4
  • 17
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    • Myllyharju J., Kivirikko K.I. Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. EMBO J. 1997, 16:1173-1180.
    • (1997) EMBO J. , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 18
    • 0016656742 scopus 로고
    • Assay of collagen-galactosyltransferase and collagen-glucosyltransferase activities and preliminary characterization of enzymic reactions with transferases from chick-embryo cartilage
    • Myllylä R., Risteli L., Kivirikko K.I. Assay of collagen-galactosyltransferase and collagen-glucosyltransferase activities and preliminary characterization of enzymic reactions with transferases from chick-embryo cartilage. Eur. J. Biochem. 1975, 52:401-410.
    • (1975) Eur. J. Biochem. , vol.52 , pp. 401-410
    • Myllylä, R.1    Risteli, L.2    Kivirikko, K.I.3
  • 20
    • 0034669227 scopus 로고    scopus 로고
    • The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion
    • Norman K.R., Moerman D.G. The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion. Dev. Biol. 2000, 227:690-705.
    • (2000) Dev. Biol. , vol.227 , pp. 690-705
    • Norman, K.R.1    Moerman, D.G.2
  • 22
    • 70350365502 scopus 로고    scopus 로고
    • Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer
    • Qian S., Waldron L., Choudhary N., Klevit R.E., Chazin W.J., Patterson C. Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer. J. Biol. Chem. 2009, 284:26797-26802.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26797-26802
    • Qian, S.1    Waldron, L.2    Choudhary, N.3    Klevit, R.E.4    Chazin, W.J.5    Patterson, C.6
  • 23
    • 0037151077 scopus 로고    scopus 로고
    • Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDaN-terminal fragment is not required for lysyl hydroxylase activity
    • Rautavuoma K., Takaluoma K., Passoja K., Pirskanen A., Kvist A.P., Kivirikko K.I., Myllyharju J. Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDaN-terminal fragment is not required for lysyl hydroxylase activity. J. Biol. Chem. 2002, 277:23084-23091.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23084-23091
    • Rautavuoma, K.1    Takaluoma, K.2    Passoja, K.3    Pirskanen, A.4    Kvist, A.P.5    Kivirikko, K.I.6    Myllyharju, J.7
  • 24
    • 4444245754 scopus 로고    scopus 로고
    • Characterization of collagenous peptides bound to lysyl hydroxylase isoforms
    • Risteli M., Niemitalo O., Lankinen H., Juffer A.H., Myllylä R. Characterization of collagenous peptides bound to lysyl hydroxylase isoforms. J. Biol. Chem. 2004, 279:37535-37543.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37535-37543
    • Risteli, M.1    Niemitalo, O.2    Lankinen, H.3    Juffer, A.H.4    Myllylä, R.5
  • 25
    • 0032808005 scopus 로고    scopus 로고
    • Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse
    • Ruotsalainen H., Sipilä L., Kerkelä E., Pospiech H., Myllylä R. Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse. Matrix Biol. 1999, 18:325-329.
    • (1999) Matrix Biol. , vol.18 , pp. 325-329
    • Ruotsalainen, H.1    Sipilä, L.2    Kerkelä, E.3    Pospiech, H.4    Myllylä, R.5
  • 28
    • 33646848764 scopus 로고    scopus 로고
    • The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration
    • Schneider V.A., Granato M. The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration. Neuron 2006, 50:683-695.
    • (2006) Neuron , vol.50 , pp. 683-695
    • Schneider, V.A.1    Granato, M.2
  • 29
    • 33846076513 scopus 로고    scopus 로고
    • Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2
    • Schneider V.A., Granato M. Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2. Matrix Biol. 2007, 26:12-19.
    • (2007) Matrix Biol. , vol.26 , pp. 12-19
    • Schneider, V.A.1    Granato, M.2
  • 30
    • 0034625345 scopus 로고    scopus 로고
    • A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum
    • Suokas M., Myllylä R., Kellokumpu S. A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum. J. Biol. Chem. 2000, 275:17863-17868.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17863-17868
    • Suokas, M.1    Myllylä, R.2    Kellokumpu, S.3
  • 31
    • 0019051354 scopus 로고
    • Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein
    • Turpeenniemi-Hujanen T.M., Puistola U., Kivirikko K.I. Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein. Biochem. J. 1980, 189:247-253.
    • (1980) Biochem. J. , vol.189 , pp. 247-253
    • Turpeenniemi-Hujanen, T.M.1    Puistola, U.2    Kivirikko, K.I.3
  • 32
    • 0019858359 scopus 로고
    • Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts
    • Turpeenniemi-Hujanen T.M., Puistola U., Kivirikko K.I. Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts. Coll. Relat. Res. 1981, 1:355-366.
    • (1981) Coll. Relat. Res. , vol.1 , pp. 355-366
    • Turpeenniemi-Hujanen, T.M.1    Puistola, U.2    Kivirikko, K.I.3
  • 33
    • 0030972003 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle
    • Valtavaara M., Papponen H., Pirttilä A.M., Hiltunen K., Helander H., Myllylä R. Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J. Biol. Chem. 1997, 272:6831-6834.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6831-6834
    • Valtavaara, M.1    Papponen, H.2    Pirttilä, A.M.3    Hiltunen, K.4    Helander, H.5    Myllylä, R.6
  • 34
    • 0032557436 scopus 로고    scopus 로고
    • Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)
    • Valtavaara M., Szpirer C., Szpirer J., Myllylä R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). J. Biol. Chem. 1998, 273:12881-12886.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12881-12886
    • Valtavaara, M.1    Szpirer, C.2    Szpirer, J.3    Myllylä, R.4
  • 35
    • 9644312354 scopus 로고    scopus 로고
    • Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)
    • Valtavaara M., Szpirer C., Szpirer J., Myllylä R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). J. Biol. Chem. 1999, 275:20956.
    • (1999) J. Biol. Chem. , vol.275 , pp. 20956
    • Valtavaara, M.1    Szpirer, C.2    Szpirer, J.3    Myllylä, R.4
  • 36
    • 0036861267 scopus 로고    scopus 로고
    • The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro
    • Wang C., Luosujärvi H., Heikkinen J., Risteli M., Uitto L., Myllylä R. The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. Matrix Biol. 2002, 21:559-566.
    • (2002) Matrix Biol. , vol.21 , pp. 559-566
    • Wang, C.1    Luosujärvi, H.2    Heikkinen, J.3    Risteli, M.4    Uitto, L.5    Myllylä, R.6
  • 37
    • 0037166347 scopus 로고    scopus 로고
    • Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3)
    • Wang C., Risteli M., Heikkinen J., Hussa A.K., Uitto L., Myllylä R. Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3). J. Biol. Chem. 2002, 277:18568-18573.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18568-18573
    • Wang, C.1    Risteli, M.2    Heikkinen, J.3    Hussa, A.K.4    Uitto, L.5    Myllylä, R.6
  • 38
    • 63049133431 scopus 로고    scopus 로고
    • The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability
    • Wang C., Kovanen V., Raudasoja P., Eskelinen S., Pospiech H., Myllylä R. The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability. J. Cell. Mol. Med. 2009, 13:508-521.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 508-521
    • Wang, C.1    Kovanen, V.2    Raudasoja, P.3    Eskelinen, S.4    Pospiech, H.5    Myllylä, R.6
  • 39
    • 0033960774 scopus 로고    scopus 로고
    • Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI
    • Yeowell H.N., Allen J.D., Walker L.C., Overstreet M.A., Murad S., Thai S.F. Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Matrix Biol. 2000, 19:37-46.
    • (2000) Matrix Biol. , vol.19 , pp. 37-46
    • Yeowell, H.N.1    Allen, J.D.2    Walker, L.C.3    Overstreet, M.A.4    Murad, S.5    Thai, S.F.6
  • 40
    • 65649108576 scopus 로고    scopus 로고
    • Cyclooxygenase allosterism, fatty acid-mediated cross-talk between monomers of cyclooxygenase homodimers
    • Yuan C., Sidhu R.S., Kuklev D.V., Kado Y., Wada M., Song I., Smith W.L. Cyclooxygenase allosterism, fatty acid-mediated cross-talk between monomers of cyclooxygenase homodimers. J. Biol. Chem. 2009, 284:10046-10055.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10046-10055
    • Yuan, C.1    Sidhu, R.S.2    Kuklev, D.V.3    Kado, Y.4    Wada, M.5    Song, I.6    Smith, W.L.7
  • 41
    • 30044442785 scopus 로고    scopus 로고
    • Calcium triggers folding of lipoprotein lipase into active dimers
    • Zhang L., Lookene A., Wu G., Olivecrona G. Calcium triggers folding of lipoprotein lipase into active dimers. J. Biol. Chem. 2005, 280:42580-42591.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42580-42591
    • Zhang, L.1    Lookene, A.2    Wu, G.3    Olivecrona, G.4


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