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Information on EC 6.3.2.4 - D-Alanine-D-alanine ligase and Organism(s) Staphylococcus aureus and UniProt Accession Q5HEB7

for references in articles please use BRENDA:EC6.3.2.4
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EC Tree
IUBMB Comments
Involved with EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase), EC 6.3.2.8 (UDP-N-acetylmuramate---L-alanine ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram).
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This record set is specific for:
Staphylococcus aureus
UNIPROT: Q5HEB7
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
d-alanine:d-alanine ligase, d-alanine-d-alanine ligase, d-ala-d-ala ligase, d-ala:d-ala ligase, vanb ligase, ttddl, abddl, tmddl, ecddlb, d-alanyl-d-alanine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Ala-D-Ala ligase
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D-Ala-D-Ala synthetase
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D-Alanine:D-alanine ligase
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D-Alanyl-D-alanine synthetase
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D-Alanylalanine synthetase
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Synthetase, D-alanylalanine
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VanA
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VanB ligase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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carboxamide formation
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
D-alanine:D-alanine ligase (ADP-forming)
Involved with EC 6.3.2.7 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase) or EC 6.3.2.13 (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase), EC 6.3.2.8 (UDP-N-acetylmuramate---L-alanine ligase), EC 6.3.2.9 (UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase) and EC 6.3.2.10 (UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase) in the synthesis of a cell-wall peptide (click here for diagram).
CAS REGISTRY NUMBER
COMMENTARY hide
9023-63-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
show the reaction diagram
ATP + Ala + Ala
?
show the reaction diagram
ATP + D-Ala + D-Ala
ADP + phosphate + D-Ala-D-Ala
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-alanine
ADP + phosphate + D-alanyl-D-alanine
show the reaction diagram
D-alanine:D-alanine ligase is an essential enzyme in bacterial cell wall biosynthesis and an important target for developing new antibiotics
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-
?
ATP + Ala + Ala
?
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-chloro-2,2-dimethyl-N-[4(trifluoromethyl)phenyl]propanamide
the inhibitor binds to a hydrophobic pocket at the interface of the first and the third domain. This inhibitor-binding pocket is adjacent to the first D-alanine substrate site but does not overlap with any substrate sites
D-cycloserine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
3-chloro-2,2-dimethyl-N-[4(trifluoromethyl)phenyl]propanamide
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Staphylococcus aureus D-alanine:D-alanine ligase and its cocrystal structures with 3-chloro-2,2-dimethyl-N-4(trifluoromethyl)phenylpropanamide and with ADP at resolutions of 2.0 A, 2.2 A, and 2.6 A, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oppenheim, B.; Patchornik, A.
Formation of D-alanyl-D-alanine and D-alanine from UDPMurNAc-L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala by extracts of Staphylococcus aureus and Streptococcus faecalis
FEBS Lett.
48
172-175
1974
Enterococcus faecalis, Staphylococcus aureus
Manually annotated by BRENDA team
Lacoste, A.M.; Poulsen, M.; Cassaigne, A.; Neuzil, E.
Inhibition of D-alanyl-D-alanine ligase in different bacterial species by amino phosphonic acids
Curr. Microbiol.
2
113-117
1979
Staphylococcus aureus, Pseudomonas aeruginosa
-
Manually annotated by BRENDA team
Liu, S.; Chang, J.S.; Herberg, J.T.; Horng, M.M.; Tomich, P.K.; Lin, A.H.; Marotti, K.R.
Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies
Proc. Natl. Acad. Sci. USA
103
15178-15183
2006
Staphylococcus aureus (Q5HEB7), Staphylococcus aureus
Manually annotated by BRENDA team