D-amino Acid Aminotransferase; Chain A, domain 1
ASP 303(Magnesium-1);GLU 316(Magnesium-1 & -2);ASN 318(Magnesium-2)
ASP 703(Magnesium-1);GLU 716(Magnesium-1 & -2);ASN 718(Magnesium-2)
ASP 257(Magnesium-1);GLU 270(Magnesium-1 & -2);ASN 272(Magnesium-2)
ATP-dependent inactivation and slow binding inhibition of Salmonella typhimurium D-alanine:D-alanine ligase (ADP) by (aminoalkyl)phosphinate and aminophosphonate analogues of D-alanine.
Synthesis of an analogue of tabtoxinine as a potential inhibitor of D-alanine:D-alanine ligase (ADP forming).
D-alanine-D-alanine ligase (ADP) from Salmonella typhimurium. Overproduction, purification, crystallization and preliminary X-ray analysis.
Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP.
Sequence of a putative glutathione synthetase II gene and flanking regions from Anaplasma centrale.
Identification of a common protease-sensitive region in D-alanyl-D-alanine and D-alanyl-D-lactate ligases and photoaffinity labeling with 8-azido ATP.
Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.
Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis.
A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.
Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B.
Evolution of structure and substrate specificity in D-alanine:D-alanine ligases and related enzymes.
Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.
D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.
D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation.
Synapsin I is structurally similar to ATP-utilizing enzymes.
Enzyme-mononucleotide interactions: three different folds share common structural elements for ATP recognition.
Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites.
The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.
Structural motif of phosphate-binding site common to various protein superfamilies: all-against-all structural comparison of protein-mononucleotide complexes.
D-Ala-D-X ligases: evaluation of D-alanyl phosphate intermediate by MIX, PIX and rapid quench studies.
Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants.
When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
Enzymes of vancomycin resistance: the structure of D-alanine-D-lactate ligase of naturally resistant Leuconostoc mesenteroides.
Sequencing of the ddl gene and modeling of the mutated D-alanine:D-alanine ligase in glycopeptide-dependent strains of Enterococcus faecium.
This enzyme is homologous to Glutathione synthetase (Swiss-prot;P04425, T00107 in EzCatDB). This enzyme catalyzes the following reactions (see [7], [8]): (A) Transfer of phosphate group from ATP to carboxyl oxygen of D-alanine, forming an intermediate, D-alanyl acylphosphate: (B) Transfer of acyl group from D-alanyl acylphosphate to amine group of the second D-alanine substrate, releasing inorganic phosphate: