Prolil hidroksilaza

Prolil hidroksilaza
Identifikatori
EC broj 1.14.11.2
CAS broj 2603-60-3
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
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PubMed articles
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Prolil hidroksilaza (prokolagen-prolin dioksigenaza) je enzim koji učestvuje u produkciji kolagena. On hidroksiliše prolin do hidrokisprolina.

Za rad prolil hidroksidaze je neophodan vitamin C kao kofaktor da bi se gvožđe održalo u redukovanom stanju (Fe2+). Vitamin C se ne konzumira stehiometrijski.[1] α-ketoglutarat služi kao redukujući agens.

Prolin + α-ketoglutarat + O2 → 4-hidroksiprolin + CO2 + sukcinat

On je klasifikovan kao EC 1.14.11.2.

Fenolno jedinjenje etil protokatehuat je inhibitor prolil 4-hidroksilaze.[2]

Reference

  1. Myllyla Raili, Tuderman Leena, Kivirikko Kari I. (1977). „Mechanism of the Prolyl Hydroxylase Reaction. 2. Kinetic Analysis of the Reaction Sequence”. European Journal of Biochemistry 80 (2): 349–57. DOI:10.1111/j.1432-1033.1977.tb11889.x. PMID 200425. 
  2. The prolyl 4-hydroxylase inhibitor ethyl-3,4-dihydroxybenzoate generates effective iron deficiency in cultured cells. Wang J, Buss JL, Chen G, Ponka P and Pantopoulos K, FEBS Lett., 2002 Oct 9, 529(2-3), pages 309-312, PMID 12372619, DOI:10.1016/S0014-5793(02)03389-6

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 
  • Berg RA, Prockop DJ (1973). „Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme”. J. Biol. Chem. 248 (4): 1175–82. PMID 4346946. 
  • Hutton JJ, Jr, Tappel AL and Udenfriend S (1967). „Cofactor and substrate requirements of collagen proline hydroxylase”. Arch. Biochem. Biophys. 118 (1): 231–240. DOI:10.1016/0003-9861(67)90302-5. 
  • Kivirikko KI, Kishida Y, Sakakibara S, Prockop DJ (1972). „Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase Effect of chain length, helical conformation and amino acid sequence in the substrate”. Biochim. Biophys. Acta. 271 (2): 347–56. PMID 5046811. 
  • Kivirikko KI and Prockop DJ (1967). „Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollogen”. Arch. Biochem. Biophys. 118 (3): 611–618. DOI:10.1016/0003-9861(67)90396-7. 

Spoljašnje veze

  • MeSH Prolyl+hydroxylase
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6