Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Kivirikko, K.I.; Myllylä, R.: The hydroxylation of prolyl and lysyl residues. Enzymol. Post-transl. Modif. Proteins (Freedman, R.B., Hawkins, H.C., eds.) Academic Press, New York, 1, 53–104 (1980)
Kivirikko, K.I.; Myllylä, R.: Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol., 82, 245–304 (1982)
Puistola, U.: Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types. Biochem. J., 201, 215–219 (1982)
Royce, P.M.; Barnes, M.J.: Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen. Biochem. J., 230, 475–480 (1985)
Puistola, U.; Turpeenniemi-Hujanen, T.M.; Myllylä, R.; Kivirikko, K.I.: Studies on the lysyl hydroxylase reaction. L Initial velocity kinetics and related aspects. Biochim. Biophys. Acta, 611, 40–50 (1980)
Puistola, U.; Turpeenniemi-Hujanen, T.M.; Myllylä, R.; Kivirikko, K.I.: Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism. Biochim. Biophys. Acta, 611, 51–60 (1980)
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., 189, 247–253 (1980)
Miller, R.L.; Varner, H.H.: Purification and enzymatic properties of lysyl hydroxylase from fetal procine skin. Biochemistry, 18, 5928–5932 (1979)
Murray, J.C.; Cassell, R.H.; Pinnell, S.R.: Inhibition of lysyl hydroxylase by catechol analogs. Biochim. Biophys. Acta, 481, 63–70 (1977)
Ryhänen, L.: Lysyl hydroxylase. Further purification and characterization of the enzyme from chick embryos and chick embryo cartilage. Biochim. Biophys. Acta, 438, 71–89 (1976)
Kivirikko, K.I.; Shudo, K.; Sakakibara, S.; Prockop, D.J.: Studies on proto-collagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate. Biochemistry, 11, 122–129 (1972)
Popenoe, E.A.; Aronson, R.B.: Partial purification and properties of collagen lysine hydroxylase from chick embryos. Biochim. Biophys. Acta, 258, 380–386 (1972)
Kivirikko, K.I.; Prockop, D.J.: Partial purification and characterization of protocollagen lysine hydroxylase from chick embryos. Biochim. Biophys. Acta, 258, 366–379 (1972)
Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latipää, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.: Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate. Biochem. J., 229, 127–133 (1985)
Hausmann E.: Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen. Biochim. Biophys. Acta, 133, 591–593 (1967)
Kellokumpu, S.; Sormunen, R.; Heikkinen, J.; Myllyla, R.: Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum. J. Biol. Chem., 269, 30524–30529 (1994)
Valtavaara, M.; Papponen, H.; Pirttilae, A.M.; Hiltunen, K.; Helander, H.; Myllylae, R.: Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J. Biol. Chem., 272, 6831–6834 (1997)
Passoja, K.; Rautavuoma, K.; Ala-Kokko, L.; Kosonen, T.; Kivirikko, K.L: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc. Natl. Acad. Sci. USA, 95, 10482–10486 (1998)
Rautavuoma, K.; Takaluoma, K.; Passoja, K.; Pirskanen, A.; Kvist, A.R; Kivirikko, K.L; Myllyharju, J.: Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1–3: The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity. J. Biol. Chem., 277, 23084–23091 (2002)
Wang, C.; Risteli, M.; Heikkinen, J.; Hussa, A.K.; Uitto, L.; Myllyla, 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., 277, 18568–18573 (2002)
Samimi, A.; Last, J.A.: Mechanism of inhibition of lysyl hydroxylase activity by the organophosphates malathion and malaoxon. Toxicol. Appl. Pharmacol., 176, 181–186 (2001)
Armstrong, L.C.; Last, J.A.: Rat lysyl hydroxylase: molecular cloning, mRNA distribution and expression in a baculovirus system. Biochim. Biophys. Acta, 1264, 93–102 (1995)
Rights and permissions
Copyright information
© 2006 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2006). Procollagen-lysine 5-dioxygenase. In: Class 1 Oxidoreductases XI. Springer Handbook of Enzymes, vol 26. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37708-5_4
Download citation
DOI: https://doi.org/10.1007/3-540-37708-5_4
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-26586-3
Online ISBN: 978-3-540-37708-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)