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Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Aspartat—prefenat aminotransferaza
Aspartat—prefenat aminotransferaza
Identifikatori
EC broj	2.6.1.78
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

Aspartat—prefenat aminotransferaza (EC 2.6.1.78, prefenatna transaminaza, PAT, prefenat aspartatna aminotransferaza, L-aspartat:prefenat aminotransferaza) je enzim sa sistematskim imenom L-arogenat:oksaloacetat aminotransferaza.^[1] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-arogenat + oksaloacetat

\rightleftharpoons

prefenat + L-aspartat

Ovaj enzim je piridoksal-fosfatni protein. Glutamat takođe deluje kao amino donor.

Reference

^ De-Eknamkul, W. & Ellis, B.E. (1988). „Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures”. Arch. Biochem. Biophys. 267: 87—94. PMID 3196038.

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.

Spoljašnje veze

Aspartate---prephenate+aminotransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] De-Eknamkul, W. & Ellis, B.E. (1988). „Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures”. Arch. Biochem. Biophys. 267: 87—94. PMID 3196038.

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