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Information on EC 6.3.2.4 - D-Alanine-D-alanine ligase and Organism(s) Mycolicibacterium smegmatis and UniProt Accession Q9ZGN0

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:
Mycolicibacterium smegmatis
UNIPROT: Q9ZGN0
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Word Map
The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
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-alanine:d-alanine (d-lactate) ligase (adp), 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
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-
?
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
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-cycloserine
0.2 mg/ml, approx. 50% inhibition, 0.8 mg/ml, approx. 80% inhibition
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDL_MYCSM
373
0
39232
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of Ddl in Mycobacterium smegmatis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feng, Z.; Barletta, R.G.
Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine
Antimicrob. Agents Chemother.
47
283-291
2003
Mycobacterium tuberculosis, Mycolicibacterium smegmatis (Q9ZGN0), Mycolicibacterium smegmatis
Manually annotated by BRENDA team