Characterization of the iron- and 2-oxoglutavate binding sites of human prolyl 4-hydroxylase

EMBO Journal

Volumn 16, Issue 6, 1997, Pages 1173-1180

  Myllyharju, Johanna ^a   Kivirikko, Kari I ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

2 oxoglutarate dependent enzymes; Catalytic site; Collagen; Dioxygenases; Non heme iron centers

Indexed keywords

2 OXOGLUTARIC ACID; HYDROXYPROLINE; IRON; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING SITE; CONTROLLED STUDY; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME SUBUNIT; HUMAN; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CONSERVED SEQUENCE; HUMANS; IRON; KETOGLUTARIC ACIDS; KINETICS; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; NUCLEOPOLYHEDROVIRUS; PROCOLLAGEN-PROLINE DIOXYGENASE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPODOPTERA;

ANIMALIA; INSECTA;

EID: 0030962028     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.6.1173     Document Type: Article

References (34)

1. Bassuk, J.A., Kao, W.W.-Y., Herzer, P., Kedersha, N.L., Seyer, J., DeMartino, J.A., Daugherty, B.L., Mark, G.E., III and Berg, R.A. (1989) Prolyl 4-hydroxylase: molecular cloning and the primary structure of the α-subunit from chicken enzyme. Proc. Natl Acad. Sci. USA, 86, 7382-7386.
2. Counts, D.F., Cardinale, G.J. and Udenfriend, S. (1978) Prolyl hydroxylase half reaction: peptidyl prolyl-independent decarboxylation of α-ketoglutarate. Proc. Natl Acad. Sci. USA, 75, 2145-2149.
3. de Jong, L. and Kemp, A. (1984) Stoichiometry and kinetics of the prolyl 4-hydroxylase partial reaction. Biochim. Biophys. Acta, 787, 105-111.
4. Gruenwald, S. and Heitz, J. (1993) Baculovirus Expression Vector System: Procedures and Methods Manual. Pharmingen, San Diego, CA.
5. Hanauske-Abel, H.M. (1991) Prolyl 4-hydroxylase, a target enzyme for drug development. Design of suppressive agents and the in vitro effects of inhibitors and proinhibitors. J. Hepatol., 13 (Suppl. 3), S8-S16.
6. Hanauske-Abel, H. and Günzler, V. (1982) A stereochemical concept for the catalytic mechanism of prolyl hydroxylase. Applicability to classification and design of inhibitors. J. Theor. Biol., 94, 421-455.
7. Helaakoski, T., Vuori, K., Myllylä, R., Kivirikko, K.I. and Pihlajamemi, T. (1989) Molecular cloning of the α-subunit of human prolyl 4-hydroxylase: The complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc. Natl Acad. Sci. USA, 86, 4392-4396.
8. 2 tetramer with the protein disulfide-isomerase/β subunit. Proc. Natl Acad. Sci. USA, 92, 4427-4431.
9. Jia, S. et al. (1994) A fully active catalytic domain of bovine aspartyl (asparaginyl) β-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate α-ketoglutarate-dependent dioxygenases. Proc. Natl Acad. Sci. USA, 91, 7227-7231.
10. Jiang, F., Peisach, J., Ming, L.-J., Que, L.J., Jr and Chen, V.J. (1991) Electron spin echo envelope modulates studies of the Cu(II)-substituted derivative of isopenicillin N synthase: a structural and spectroscopic model. Biochemists, 30, 11437-11445.
11. Kivirikko, K.I. and Myllylä, R. (1982) Post-translational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol., 82, 245-304.
12. Kivirikko, K.I., Myllylä, R. and Pihlajaniemi, T. (1989) Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. FASEB J., 3, 1609-1617.
13. Kivirikko, K.I., Myllylä, R. and Pihlajaniemi, T. (1992) Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In Harding, J.J. and Crabbe, M.J.C. (eds), Post-translational Modifications of Proteins. CRC Press, Boca Raton, FL, pp. 1-51.
14. Koivu, J., Myllylä, R., Helaakoski, T., Pihlajaniemi, T., Tasanen, K. and Kivirikko, K.I. (1987) A single polypeptide acts both as the β subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J. Biol. Chem., 262, 6447-6449.
15. Lamberg, A., Pihlajaniemi, T. and Kivirikko, K.I. (1995) Site-directed mutagenesis of the α subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity. J. Biol. Chem., 270, 9926-9931.
16. Majamaa, K., Hanauske-Abel, H.M., Günzler, V. and Kivirikko, K.I. (1984) The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion. Eur. J. Biochem., 138, 239-245.
17. Majamaa, K., Günzler, V., Hanauske-Abel, H.M., Myllylä, R. and Kivirikko, K.I. (1986) Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J. Biol. Chem., 261, 7819-7823.
18. 2+. Biochemistry, 35, 3957-3962.
19. Ming, L.-J., Que, L.J., Jr, Kriauciunas, A., Frolik, C.A. and Chen, V.J. (1991) NMR studies of the active site of isopenicillin N synthase, a non-heme iron(II) enzyme. Biochemistry, 30, 11653-11659.
20. Myllylä, R., Tuderman, L. and Kivirikko, K.I. (1977) Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence. Eur. J. Biochem., 80, 349-357.
21. Myllylä, R., Majamaa, K., Günzler, V., Hanauske-Abel, H.M. and Kivirikko, K.I. (1984) Ascorbate is consumed stoichiomemcally in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem., 259, 5403-5405.
22. Myllylä, R., Pihlajaniemi, T., Pajunen, L., Turpeenniemi-Hujanen, T. and Kivirikko, K.I. (1991) Molecular cloning of chick lysyl hydroxylase. Little homology in primary structure to the two types of subunit of prolyl 4-hydroxylase. J. Biol. Chem., 266, 2805-2810.
23. Myllylä, R., Günzler, V., Kivirikko, K.I. and Kaska, D.D. (1992) Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl-pyrocarbonate: evidence for histidine residues in the catalytic site of 2-oxoglutarate coupled dioxygenases. Biochem. J., 286, 923-927.
24. Parkkonen, T., Kivirikko, K.I. and Pihlajaniemi, T. (1988) Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase β-subunit, protein disulphide isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species. Biochem. J., 256, 1006-1011.
25. Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M.-L., Koivu, J. and Kivirikko, K.I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J., 6, 643-649.
26. Pirskanen, A., Kaimio, A.-M., Myllylä, R. and Kivirikko, K.I. (1996) Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. J. Biol. Chem., 271, 9398-9402.
27. Prockop, D.J. and Kivirikko, K.I. (1995) Collagens: molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem., 64, 403-434.
28. Randall, C.R., Zang, Y., True, A.E., Que, L.J., Jr, Charnock, J.M., Garner, C.D., Fujishima, Y., Schofield, C.J. and Baldwin, J.E. (1993) X-ray absorption studies of the ferrous active site of isopenicillin N synthase and related model complexes. Biochemistry, 32, 6664-6673.
29. n stimulates α-ketoglutarate decarboxylation without prolyl hydroxylation. J. Biol. Chem., 253, 6327-6330.
30. Roach, P.L., Clifton, I.J., Fülöp, V., Harlos, K., Barton, G.J., Hajdu, J., Andersson, I., Schofield, C.J. and Baldwin, J.E. (1995) Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature, 375, 700-704.
31. Sanger, K., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA, 74, 5463-5467.
32. Tuderman, L., Myllylä, R. and Kivirikko, K.I. (1977) Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates. Eur. J. Biochem., 80, 341-348.
33. Veijola, J., Koivunen, P., Annunen, P., Pihlajaniemi, T. and Kivirikko, K.I. (1994) Cloning, baculovirus expression, and characterization of the α-subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This α-subunit forms an active αβ dimer with the human protein disulfide isomerase/β subunit. J. Biol. Chem., 269, 26746-26753.
34. Vuori, K., Pihlajaniemi, T., Marttila, M. and Kivirikko, K.I. (1992) Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide isomerase subunit synthesized in a baculovirus system. Proc. Natl Acad. Sci. USA, 89, 7467-7470.