Cistationinska g-lijaza
| Cistationinska g-lijaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Cistationinska g-lijaza tetramer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 4.4.1.1 | ||||||||
| CAS broj | 9012-96-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Cistationinska g-lijaza (EC 4.4.1.1, homoserinska deaminaza, homoserinska dehidrataza, cistinska desulfhidraza, cisteinska desulfhidraza, gama-cistationaza, cistationaza, homoserinska deaminaza-cistationaza, gama-CTL, cistalisin, L-cistationinska cistein-lijaza (deaminacija)) je enzim sa sistematskim imenom L-cistationin cistein-lijaza (deaminacija, formira 2-oksobutanoat).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-cistationin + H2O L-cistein + NH3 + 2-oksobutanoat (sveukupna reakcija);;
- (1a) L-cistationin L-cistein + 2-amoniobut-2-enoat
- (1b) 2-amoniobut-2-enoat + H2O 2-oksobutanoat + NH3 (sponta reakcija)
Ovaj enzim je multifunkcionalni piridoksal-fosfatni protein.
Reference
- ↑ Braunstein, A.E. and Azarkh, R.M. (1950). „[Participation of vitamin B6 in enzymic formation of hydrogen sulfide from L-cysteine.]”. Dokl. Akad. Nauk. S.S.S.R. 71: 93-96.
- ↑ Braunstein, A.E. and Azarkh, R.M. (1952). „[Phosphopyridoxal in aerobic deamination of homoserine and serine.]”. Dokl. Akad. Nauk. S.S.S.R. 85: 385-388.
- ↑ Flavin, M. and Segal, A. (1964). „Purification and properties of the cystathionine γ-cleavage enzyme of Neurospora”. J. Biol. Chem. 239: 2220-2227. PMID 14209951.
- ↑ Matsuo, Y. and Greenberg, D.M. (1959). „A crystalline enzyme that cleaves homoserine and cystathionine. III. Coenzyme resolution, activation, and inhibitors”. J. Biol. Chem. 234: 507-515. PMID 13641250.
- ↑ Matsuo, Y. and Greenberg, D.M. (1959). „A crystalline enzyme that cleaves homoserine and cystathionine. IV. Mechanism of action, reversibility, and substrate specificity”. J. Biol. Chem. 234: 516-519. PMID 13641251.
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.
Spoljašnje veze
- MeSH Cystathionine+gamma-lyase
- 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
