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D-aspartatna ligaza
Identifikatori
EC broj	6.3.1.12
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

D-aspartatna ligaza (EC 6.3.1.12, Aslfm, UDP-MurNAc-pentapeptid:D-aspartat ligaza, D-aspartinska kiselina-aktivirajući enzim) je enzim sa sistematskim imenom D-aspartat:(beta-GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lis-D-Ala-D-Ala))_n ligaza (formira ADP).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + D-aspartat + [beta-GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala)]_n

\rightleftharpoons

[beta-GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]ⁿ + ADP + fosfat

Ovaj enzim formira deo puta peptidoglikanskog formiranja kod Gram-pozitivnih bakterija.

Reference

↑ Staudenbauer, W. and Strominger, J.L. (1972). „Activation of D-aspartic acid for incorporation into peptidoglycan”. J. Biol. Chem. 247: 5095-5102. PMID 4262567.
↑ Staudenbauer, W., Willoughby, E. and Strominger, J.L. (1972). „Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane”. J. Biol. Chem. 247: 5289-5296. PMID 4626717.
↑ Galperin, M.Y. and Koonin, E.V. (1997). „A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity”. Protein Sci. 6: 2639-2643. PMID 9416615.
↑ Bellais, S., Arthur, M., Dubost, L., Hugonnet, J.E., Gutmann, L., van Heijenoort, J., Legrand, R., Brouard, J.P., Rice, L. and Mainardi, J.L. (2006). „Asl_fm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium”. J. Biol. Chem. 281: 11586-11594. PMID 16510449.

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 D-aspartate+ligase

[1] Staudenbauer, W. and Strominger, J.L. (1972). „Activation of D-aspartic acid for incorporation into peptidoglycan”. J. Biol. Chem. 247: 5095-5102. PMID 4262567.

[2] Staudenbauer, W., Willoughby, E. and Strominger, J.L. (1972). „Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane”. J. Biol. Chem. 247: 5289-5296. PMID 4626717.

[3] Galperin, M.Y. and Koonin, E.V. (1997). „A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity”. Protein Sci. 6: 2639-2643. PMID 9416615.

[4] Bellais, S., Arthur, M., Dubost, L., Hugonnet, J.E., Gutmann, L., van Heijenoort, J., Legrand, R., Brouard, J.P., Rice, L. and Mainardi, J.L. (2006). „Asl_fm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium”. J. Biol. Chem. 281: 11586-11594. PMID 16510449.

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