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PMC	članci
PubMed	članci
NCBI	proteini

Tirozin 3-monooksigenaza
Tirozin 3-monooksigenaza
Identifikatori
EC broj	1.14.16.2
CAS broj	9036-22-0
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Tirozin 3-monooksigenaza (EC 1.14.16.2, L-tirozinska hidroksilaza, tirozinska 3-hidroksilaza, tirozinska hidroksilaza) je enzim sa sistematskim imenom L-tirozin,tetrahidrobiopterin:kiseonik oksidoreduktaza (3-hidroksilacija).^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-tirozin + tetrahidrobiopterin + O₂

\rightleftharpoons

L-dopa + 4a-hidroksitetrahidrobiopterin

Aktivni centar sadrži mononuklearno gvožđe(II). Ovaj enzim se aktivira fosforilacijom.

Reference

^ El Mestikawy, S., Glowinski, J. and Hamon, M. (1983). „Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca²⁺-dependent phosphorylation”. Nature (Lond.). 302: 830—832. PMID 6133218.
^ Ikeda, M., Levitt, M. and Udenfriend, S. (1967). „Phenylalanine as substrate and inhibitor of tyrosine hydroxylase”. Arch. Biochem. Biophys. 120: 420—427. PMID 6033458.
^ Nagatsu, T., Levitt, M. and Udenfriend, S. (1964). „Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis”. J. Biol. Chem. 239: 2910—2917. PMID 14216443.
^ Pigeon, D., Drissi-Daoudi, R., Gros, F. and Thibault, J. (1986). „Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase”. C. R. Acad. Sci. III. 302: 435—438. PMID 2872947.
^ Goodwill, K.E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P.F. and Stevens, R.C. (1997). „Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases”. Nat. Struct. Biol. 4: 578—585. PMID 9228951.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Tyrosine+3-monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] El Mestikawy, S., Glowinski, J. and Hamon, M. (1983). „Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca²⁺-dependent phosphorylation”. Nature (Lond.). 302: 830—832. PMID 6133218.

[2] Ikeda, M., Levitt, M. and Udenfriend, S. (1967). „Phenylalanine as substrate and inhibitor of tyrosine hydroxylase”. Arch. Biochem. Biophys. 120: 420—427. PMID 6033458.

[3] Nagatsu, T., Levitt, M. and Udenfriend, S. (1964). „Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis”. J. Biol. Chem. 239: 2910—2917. PMID 14216443.

[4] Pigeon, D., Drissi-Daoudi, R., Gros, F. and Thibault, J. (1986). „Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase”. C. R. Acad. Sci. III. 302: 435—438. PMID 2872947.

[5] Goodwill, K.E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P.F. and Stevens, R.C. (1997). „Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases”. Nat. Struct. Biol. 4: 578—585. PMID 9228951.

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