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PMID: 2557001 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The catalytic mechanism of the hydroxylation reaction of peptidyl proline and lysine does not require protein disulphide-isomerase activity.

The Biochemical journal ·Vol. 263 ·No. 2 ·1989-10-15 ·Pages 609-11

Myllylä R, Kaska DD, Kivirikko KI

Abstract

Prolyl 4-hydroxylase, an alpha 2 beta 2 tetramer, catalyses the formation of 4-hydroxyproline in collagens. The beta subunit is known to be identical with the enzyme protein disulphide-isomerase and to possess disulphide-isomerase activity even when present in the prolyl 4-hydroxylase tetramer. We here report that lysyl hydroxylase, a homodimer, and algal prolyl 4-hydroxylase, a monomer, do not contain detectable protein disulphide-isomerase activity. Since the hydroxylase reaction mechanisms are similar, the data suggest that the protein disulphide-isomerase activity of the vertebrate prolyl 4-hydroxylase beta subunit is unlikely to be involved in the catalytic mechanism of the hydroxylation reaction.

MeSH Terms
Animals Catalysis Chick Embryo Chlamydomonas/enzymology Hydroxylation Isomerases/metabolism Lysine/metabolism Macromolecular Substances Mixed Function Oxygenases/metabolism Molecular Weight Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase/metabolism Procollagen-Proline Dioxygenase/metabolism Proline/metabolism Protein Disulfide-Isomerases
Chemicals
Macromolecular Substances Proline Mixed Function Oxygenases Procollagen-Proline Dioxygenase Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase Isomerases Protein Disulfide-Isomerases Lysine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Myllylä R
Collagen Research Unit, University of Oulu, Finland.
Kaska D D
Kivirikko K I
References (26)
26 references, click to expand
  1. Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins.
    Biochem Soc Trans. 1988 Apr;16(2):96-9 PMID: 3371540
  2. Recent developments in posttranslational modification: intracellular processing.
    Methods Enzymol. 1987;144:96-114 PMID: 3041180
  3. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes.
    Nature. 1988 Oct 13;335(6191):649-51 PMID: 3173483
  4. Polyclonal and monoclonal antibodies to human lysyl hydroxylase and studies on the molecular heterogeneity of the enzyme.
    Biochem J. 1988 Jul 15;253(2):489-96 PMID: 3140780
  5. Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the alpha subunit of the vertebrate enzyme.
    Biochem J. 1988 Nov 15;256(1):257-63 PMID: 2851981
  6. Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.
    FASEB J. 1989 Mar;3(5):1609-17 PMID: 2537773
  7. Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates.
    Eur J Biochem. 1977 Nov 1;80(2):341-8 PMID: 200424
  8. Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence.
    Eur J Biochem. 1977 Nov 1;80(2):349-57 PMID: 200425
  9. Some characteristics of protein disulfide isomerase (E.C.5.3.4.1) from wheat (Triticum vulgare) embryo.
    Biochimie. 1978 Sep 4;60(5):547-51 PMID: 698293
  10. Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects.
    Biochim Biophys Acta. 1980 Jan 11;611(1):40-50 PMID: 6766066
  11. Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism.
    Biochim Biophys Acta. 1980 Jan 11;611(1):51-60 PMID: 6766067
  12. Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein.
    Biochem J. 1980 Aug 1;189(2):247-53 PMID: 6779811
  13. A rapid and sensitive assay for protein disulphide isomerase activity.
    J Biochem Biophys Methods. 1983 Feb;7(2):115-21 PMID: 6187793
  14. Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase.
    Methods Enzymol. 1984;107:281-94 PMID: 6503714
  15. Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate.
    Biochem J. 1985 Jul 1;229(1):127-33 PMID: 2994628
  16. Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase.
    Biochem J. 1976 Nov;159(2):377-84 PMID: 11783
  17. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.
    Nature. 1985 Sep 19-25;317(6034):267-70 PMID: 3840230
  18. Photoaffinity labeling of peptide binding sites of prolyl 4-hydroxylase with N-(4-azido-2-nitrophenyl)glycyl-(Pro-Pro-Gly)5.
    Biochemistry. 1985 Nov 5;24(23):6493-9 PMID: 3002443
  19. Post-translational processing of procollagens.
    Ann N Y Acad Sci. 1985;460:187-201 PMID: 3008623
  20. Protein disulfide-isomerase retains procollagen prolyl 4-hydroxylase structure in its native conformation.
    Biochemistry. 1986 Oct 7;25(20):5982-6 PMID: 3024699
  21. Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation.
    J Biol Chem. 1987 May 5;262(13):6159-64 PMID: 3571251
  22. A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase.
    J Biol Chem. 1987 May 15;262(14):6447-9 PMID: 3032969
  23. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.
    EMBO J. 1987 Mar;6(3):643-9 PMID: 3034602
  24. Characterization of a low-relative-molecular-mass prolyl 4-hydroxylase from the green alga Chlamydomonas reinhardii.
    Biochem J. 1987 Jan 15;241(2):483-90 PMID: 3036064
  25. Time-dependent inactivation of chick-embryo prolyl 4-hydroxylase by coumalic acid. Evidence for a syncatalytic mechanism.
    Biochem J. 1987 Feb 15;242(1):163-9 PMID: 3036081
  26. Syncatalytic inactivation of prolyl 4-hydroxylase by anthracyclines.
    Biochem J. 1988 Apr 15;251(2):365-72 PMID: 2840891
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2630609
Published
1989-10-15
Pages
609-11
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1133471
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2630609 PMC Full Text View journal details
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