Transketolaza
Transketolaza | |||||||||
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Transketolaza dimer, Human | |||||||||
Identifikatori | |||||||||
EC broj | 2.2.1.1 | ||||||||
CAS broj | 9014-48-6 | ||||||||
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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Transketolaza (EC 2.2.1.1, glikolaldehidtransferaza) je enzim sa sistematskim imenom sedoheptuloza-7-fosfat:D-gliceraldehid-3-fosfat glikolaldehidtransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- sedoheptuloza 7-fosfat + D-gliceraldehid 3-fosfat D-riboza 5-fosfat + D-ksiluloza 5-fosfat
Ovaj enzim je tiamin-difosfatni protein. On ima široku specifičnost za reaktante, e.g. konvertuje hidroksipiruvat i R-CHO u CO2 i R-CHOH-CO-CH2OH. Transketolaza iz Alkaligenes faecalis je veoma aktivna sa D-eritrozom kao akceptorom.
Reference
- ↑ De La Haba, G., Leder, I.G and Racker, E. (1955). „Crystalline transketolase from bakers' yeast: isolation and properties”. J. Biol. Chem. 214: 409-426. PMID 14367398.
- ↑ Domagk, G.F. and Horecker, B.L. (1965). „Fructose and erythrose metabolism in Alcaligenes faecalis”. Arch. Biochem. Biophys. 109: 342-349.
- ↑ Horecker, B.L., Smyrniotis, P.Z. and Hurwitz, J. (1956). „The role of xylulose 5-phosphate in the transketolase reaction”. J. Biol. Chem. 223: 1009-1019. PMID 13385248.
- ↑ Racker, E. (1961). „Transketolase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 5 (2nd izd.). New York: Academic Press. str. 397-412.
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.
- Racker, E. (1961). „Transketolase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 5 (2nd izd.). New York: Academic Press. str. 397-412.
Spoljašnje veze
- MeSH Transketolase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
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