Asparaginska sintaza (glutamin-hidrolizujuća)

Asparaginska sintaza (glutamin-hidrolizujuća)
Asparaginska sintetaza B, dimer, E.Coli
Identifikatori
EC broj	6.3.5.4
CAS broj	37318-72-2
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga PMC articles PubMed articles NCBI Protein search

Asparaginska sintaza (glutamin-hidrolizujuća) (EC 6.3.5.4, asparaginska sintetaza (glutaminska hidroliza), glutamin-zavisna asparaginska sintetaza, asparaginska sintetaza B, AS, AS-B) je enzim sa sistematskim imenom L-aspartat:L-glutamin amido-ligaza (formira AMP).^{[1][2][3][4][5][6]} Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + L-aspartat + L-glutamin + H₂O ${\displaystyle \rightleftharpoons }$ AMP + difosfat + L-asparagin + L-glutamat (sveukupna reakcija)

(1a) L-glutamin + H₂O ${\displaystyle \rightleftharpoons }$ L-glutamat + NH₃

(1b) ATP + L-aspartat + NH₃ ${\displaystyle \rightleftharpoons }$ AMP + difosfat + L-asparagin

Enzim iz Escherichia coli ima dva aktivna mesta.

Reference

1. Patterson, M.K., Jr. and Orr, G.R. (1968). „Asparagine biosynthesis by the Novikoff hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system”. J. Biol. Chem. 243: 376-380. PMID 4295091. 
2. Boehlein, S.K., Richards, N.G. and Schuster, S.M. (1994). „Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad”. J. Biol. Chem. 269: 7450-7457. PMID 7907328. 
3. Richards, N.G. and Schuster, S.M. (1998). „Mechanistic issues in asparagine synthetase catalysis”. Adv. Enzymol. Relat. Areas Mol. Biol. 72: 145-198. PMID 9559053. 
4. Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G., Thoden, J.B., Holden, H.M. and Rayment, I. (1999). „Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product”. Biochemistry 38: 16146-16157. PMID 10587437. 
5. Huang, X., Holden, H.M. and Raushel, F.M. (2001). „Channeling of substrates and intermediates in enzyme-catalyzed reactions”. Annu. Rev. Biochem. 70: 149-180. PMID 11395405. 
6. Tesson, A.R., Soper, T.S., Ciustea, M. and Richards, N.G. (2003). „Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli”. Arch. Biochem. Biophys. 413: 23-31. PMID 12706338. 

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. 

Vanjske veze

• MeSH Asparagine+synthase+(glutamine-hydrolysing)