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PubMed	članci
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Triptofan transaminaza
Triptofan transaminaza
Identifikatori
EC broj	2.6.1.27
CAS broj	9022-98-4
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

Triptofan transaminaza (EC 2.6.1.27, L-fenilalanin-2-oksoglutaratna aminotransferaza, triptofanska aminotransferaza, 5-hidroksitriptofan-ketoglutarinska transaminaza, hidroksitriptofanska aminotransferaza, L-triptofanska aminotransferaza, L-triptofanska transaminaza) je enzim sa sistematskim imenom L-triptofan:2-oksoglutarat aminotransferaza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-triptofan + 2-oksoglutarat

\rightleftharpoons

(indol-3-il)piruvat + L-glutamat

Oksaloacetat može da zameni 2-oksoglutarat. On takođe deluje na 5-hidroksitriptofan i u manjoj meri na fenilne aminokiseline.

Reference

^ George, H. & Gabay, S. (1968). „Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase”. Biochim. Biophys. Acta. 167: 555—566. PMID 5722279.
^ O'Neil, S.R. & DeMoss, R.D. (1968). „Tryptophan transaminase from Clostridium sporogenes”. Arch. Biochem. Biophys. 127: 361—368. PMID 5697992.
^ Tangen, O., Fonnum, F. and Haavaldsen, R. (1965). „Separation and purification of aromatic amino acid transaminases from rat brain”. Biochim. Biophys. Acta. 96: 82—90. PMID 14285270.

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

Tryptophan+transaminase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] George, H. & Gabay, S. (1968). „Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase”. Biochim. Biophys. Acta. 167: 555—566. PMID 5722279.

[2] O'Neil, S.R. & DeMoss, R.D. (1968). „Tryptophan transaminase from Clostridium sporogenes”. Arch. Biochem. Biophys. 127: 361—368. PMID 5697992.

[3] Tangen, O., Fonnum, F. and Haavaldsen, R. (1965). „Separation and purification of aromatic amino acid transaminases from rat brain”. Biochim. Biophys. Acta. 96: 82—90. PMID 14285270.

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