Aspartat kinaza

Izvor: Wikipedia
Aspartat kinaza
Identifikatori
EC broj 2.7.2.4
CAS broj 9012-50-4
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures

Aspartat kinaza (EC 2.7.2.4, aspartokinaza, AK, beta-aspartokinaza, aspartinska kinaza) je enzim sa sistematskim imenom ATP:L-aspartat 4-fosfotransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + L-aspartat \rightleftharpoons ADP + 4-fosfo-L-aspartat

Enzim iz Escherichia coli je multifunkcionalni protein, koji takođe katalizuje reakciju EC 1.1.1.3, homoserin dehidrogenaze.

Reference[uredi - уреди]

  1. Black, S. (1962). "Conversion of aspartic acid to homoserine". Methods Enzymol. 5: 820–827. 
  2. Paulus, H. and Gray, E. (1967). "Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies". J. Biol. Chem. 242: 4980–4986. PMID 6058940. 
  3. Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. (1972). "Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex". Biochemistry 11: 677–687. PMID 4551091. 
  4. Véron, M., Falcoz-Kelly, F. and Cohen, G.N. (1972). "The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain". Eur. J. Biochem. 28: 520–527. PMID 4562990. 
  5. Chassagnole, C., Rais, B., Quentin, E., Fell, D. A. and Mazat, J.-P. (2001). "An integrated study of threonine-pathway enzyme kinetics in Escherichia coli". Biochem. J. 356: 415–423. 
  6. Curien, G., Ravanel, S., Robert, M. and Dumas, R. (2005). "Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms". J. Biol. Chem. 280: 41178–41183. 

Literatura[uredi - уреди]

Vanjske veze[uredi - уреди]