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Literature summary for 6.3.2.4 extracted from

  • Yang, S.; Xu, Y.; Wang, Y.; Ren, F.; Li, S.; Ding, W.; Ma, Y.; Zhang, W.
    The biological properties and potential interacting proteins of D-alanyl-D-alanine ligase a from Mycobacterium tuberculosis (2018), Molecules, 23, 324-338 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.2.4

Application

Application Comment Organism
drug development the enzyme is a target for drug development to combat against Mycobacterium tuberculosis (Mtb) Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
gene ddlA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
D-cycloserine a competitive inhibitor Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics Mycobacterium tuberculosis
0.0503
-
 ATP pH 8.0, 37°C, recombinant His-tagged enzyme Mycobacterium tuberculosis
1.011
-
 D-alanine pH 8.0, 37°C, recombinant His-tagged enzyme Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 2 D-alanine Mycobacterium tuberculosis
-
 ADP + phosphate + D-alanyl-D-alanine
-
 ?
ATP + 2 D-alanine Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
 ADP + phosphate + D-alanyl-D-alanine
-
 ?
additional information Mycobacterium tuberculosis putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview ?
-
 ?
additional information Mycobacterium tuberculosis ATCC 25618 / H37Rv putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WP31
-
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv P9WP31
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine first, the ATP-dependent dimerization reactions catalyzed by DdlA proceed through the phosphorylation of the D-alanine at the carboxyl group by the gamma-phosphate of ATP to produce an acylphosphate intermediate. Then, a tetrahedral intermediate is formed by the nucleophilic attacking of the amino nitrogen of the second D-alanine on the acylphosphate intermediate. Finally, a phosphate group is released from the tetrahedral intermediate to generate the final product of D-alanyl-D-alanine Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2 D-alanine
-
 Mycobacterium tuberculosis ADP + phosphate + D-alanyl-D-alanine
-
 ?
ATP + 2 D-alanine DdlA catalyzes the dimerization of two D-alanine molecules and typically couples ATP hydrolysis to provide a thermodynamic driving force and exhibits a cleavage of ATP to ADP and phosphate. D-Alanine is completely converted into D-alanyl-D-alanine, so no remaining D-alanine is detected Mycobacterium tuberculosis ADP + phosphate + D-alanyl-D-alanine
-
 ?
ATP + 2 D-alanine
-
 Mycobacterium tuberculosis ATCC 25618 / H37Rv ADP + phosphate + D-alanyl-D-alanine
-
 ?
ATP + 2 D-alanine DdlA catalyzes the dimerization of two D-alanine molecules and typically couples ATP hydrolysis to provide a thermodynamic driving force and exhibits a cleavage of ATP to ADP and phosphate. D-Alanine is completely converted into D-alanyl-D-alanine, so no remaining D-alanine is detected Mycobacterium tuberculosis ATCC 25618 / H37Rv ADP + phosphate + D-alanyl-D-alanine
-
 ?
additional information putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview Mycobacterium tuberculosis ?
-
 ?
additional information putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview Mycobacterium tuberculosis ATCC 25618 / H37Rv ?
-
 ?

Subunits

Subunits Comment Organism
? x * 39680, sequence calculation, x * 40000, about, recombinant His-tagged enzyme, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
DdlA
-
 Mycobacterium tuberculosis
Rv2981c
-
 Mycobacterium tuberculosis
Tb-DdlA
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00073
-
 ATP pH 8.0, 37°C, recombinant His-tagged enzyme Mycobacterium tuberculosis
0.00073
-
 D-alanine pH 8.0, 37°C, recombinant His-tagged enzyme Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism two different metabolic pathways, of DdlA and LysA, respectively, leading to peptidoglycan biosynthesis, overview Mycobacterium tuberculosis
physiological function D-alanine-D-alanine ligase (DdlA) supplies D-alanyl-D-alanine as a substrate for peptidoglycan crosslinking by catalyzing the dimerization of two D-alanines, the enzyme is involved in the pentapeptide biosynthesis of peptidoglycan Mycobacterium tuberculosis