Function: ddl enzymes are part of the ATP-grasp superfamily and play a vital role in bacterial cell wall synthesis by forming the d-alanyl--d-alanine dipeptide .
Structure: The enzyme consists of an N-terminal, central, and C-terminal domain, with each subunit possessing a single ATP-binding site and two d-Ala binding sites .
Importance: ddl is a target for antibiotics like d-cycloserine, used in treating multi-drug-resistant tuberculosis .
D-cycloserine Resistance: Variants of ddl have been found to confer resistance to d-cycloserine, an antibiotic used for treating multi-drug-resistant tuberculosis .
Vancomycin Resistance: ddl can serve as a marker to predict vancomycin resistance in certain bacteria, as it influences peptidoglycan composition .
Broad Substrate Specificity: Some ddl enzymes, like those from Escherichia coli and Thermotoga maritima, show broad substrate specificity for various D-amino acids .
Counterselection Marker: ddl has been used as a counterselection marker in genetic engineering of lactic acid bacteria to enhance genome editing efficiency .
While specific information on "Recombinant Nitrosomonas europaea D-alanine--D-alanine ligase (ddl)" is not available, the general study of ddl enzymes highlights their potential in biotechnology and antibiotic resistance research. Future studies could explore the cloning and characterization of ddl from Nitrosomonas europaea to understand its unique properties and potential applications.
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Cell wall formation.
KEGG: neu:NE0994
STRING: 228410.NE0994