D-aspartate ligase

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D-aspartate ligase
Identifiers
EC number
6.3.1.12
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG
KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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In enzymology, a D-aspartate ligase (EC 6.3.1.12) is an enzyme that catalyzes th
e chemical reaction
ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala
-D- Ala)]n \rightleftharpoons [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6
-N-(beta-D-Asp)-L- Lys-D-Ala-D-Ala)]n + ADP + phosphate
The 4 substrates of this enzyme are ATP, D-aspartate, [[beta-GlcNAc-(1->4)-Mur2A
c(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-]], and [[Ala)]n]], whereas its 4 products
are [[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-]], [[
Lys-D-Ala-D-Ala)]n]], ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbonnitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The syste
matic name of this enzyme class is D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-LAla-gamma-D-Glu-L-Lys-D -Ala-D-Ala)]n ligase (ADP-forming). Other names in commo
n use include Aslfm, UDP-MurNAc-pentapeptide:D-aspartate ligase, and D-aspartic
acid-activating enzyme.
References[edit]
Staudenbauer W, Strominger JL (1972). "Activation of D-aspartic acid for incorpo
ration into peptidoglycan". J. Biol. Chem. 247 (16): 5095 102. PMID 4262567.
Staudenbauer W, Willoughby E, Strominger JL (1972). "Further studies of the D-as
partic acid-activating enzyme of Streptococcus faecalis and its attachment to th
e membrane". J. Biol. Chem. 247 (17): 5289 96. PMID 4626717.
Galperin MY, Koonin EV (1997). "A diverse superfamily of enzymes with ATP-depend
ent carboxylate-amine/thiol ligase activity". Protein. Sci. 6 (12): 2639 43. doi:1
0.1002/pro.5560061218. PMC 2143612. PMID 9416615.
Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL (2006). "Aslfm, the D-a
spartate ligase responsible for the addition of D-aspartic acid onto the peptido
glycan precursor of Enterococcus faecium". J. Biol. Chem. 281 (17): 11586 94. doi:
10.1074/jbc.M600114200. PMID 16510449.
This ligase article is a stub. You can help Wikipedia by expanding it.
Categories: EC 6.3.1Enzymes of unknown structureLigase stubs
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