Enzyme

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     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases)
ID:6.3.1.12
Description:D-aspartate ligase.
Alternative Name: D-aspartic acid-activating enzyme.
Asl(fm).
Prosite: PDOC50975;
PDB:
PDBScop

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.1.12
BRENDA Enzyme Link: BRENDA 6.3.1.12
KEGG Enzyme Link: KEGG6.3.1.12
BioCyc Enzyme Link: BioCyc 6.3.1.12
ExPASy Enzyme Link: ExPASy6.3.1.12
EC2PDB Enzyme Link: EC2PDB 6.3.1.12
ExplorEnz Enzyme Link: ExplorEnz 6.3.1.12
PRIAM enzyme-specific profiles Link: PRIAM 6.3.1.12
IntEnz Enzyme Link: IntEnz 6.3.1.12
MEDLINE Enzyme Link: MEDLINE 6.3.1.12
MSA:

6.3.1.12;

Phylogenetic Tree:

6.3.1.12;

Uniprot:
M-CSA:
RHEA:10752 [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n) + n ATP + n D-aspartate = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n H(+) + n phosphate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.Galperin MY, Koonin EV1997 Dec9416615
Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane.Staudenbauer W, Willoughby E, Strominger JL1972 Sep 104626717
Activation of D-aspartic acid for incorporation into peptidoglycan.Staudenbauer W, Strominger JL1972 Aug 254262567
Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium.Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL2006 Apr 2816510449