Literature summary extracted from

Shi, Y.; Walsh, C.T.
Active site mapping of Escherichia coli D-Ala-D-Ala ligase by structure-based mutagenesis (1995), Biochemistry, 34, 2768-2776.

Protein Variants

EC Number	Protein Variants	Comment	Organism
6.3.2.4	additional information	mutant enzymes at K144, K215, and E270 in the ATP binding site, at E15, S150, H63, and R255 in the first D-Ala subsite, and at Y216, S281, L282, and D257 in the second D-Ala subsite. Mutant enzymes E270Q, K215A, R255A, and D257N retain very low or no detectable activity. Mutants enzyme Y216F shows substantial retention of activity	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.3.2.4	Phosphinates	-	Escherichia coli

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
6.3.2.4	0.0012	-	D-Ala	N-terminal Ala, wild-type enzyme	Escherichia coli
6.3.2.4	0.008	-	ATP	mutant enzyme Y216K	Escherichia coli
6.3.2.4	0.033	-	ATP	mutant enzyme Y216F	Escherichia coli
6.3.2.4	0.049	-	ATP	wild-type enzyme	Escherichia coli
6.3.2.4	0.055	-	ATP	mutant enzyme E15Q	Escherichia coli
6.3.2.4	0.161	-	ATP	mutant enzyme H63Q	Escherichia coli
6.3.2.4	0.179	-	ATP	mutant enzyme S150A	Escherichia coli
6.3.2.4	0.26	-	D-Ala	N-terminal Ala, mutant enzyme Y216F	Escherichia coli
6.3.2.4	0.43	-	D-Ala	N-terminal Ala, mutant enzyme E15Q, mutant enzyme Y216K	Escherichia coli
6.3.2.4	0.49	-	D-Ala	N-terminal Ala, mutant enzyme L282R	Escherichia coli
6.3.2.4	0.55	-	D-Ala	N-terminal Ala, mutant enzyme H63Q	Escherichia coli
6.3.2.4	0.76	-	D-Ala	N-terminal Ala, mutant enzyme S150A	Escherichia coli
6.3.2.4	1.05	-	D-Ala	C-terminal Ala, mutant enzyme D257N	Escherichia coli
6.3.2.4	1.13	-	D-Ala	C-terminal Ala, wild-type enzyme	Escherichia coli
6.3.2.4	2.4	-	ATP	mutant enzyme K144A	Escherichia coli
6.3.2.4	2.5	-	ATP	mutant enzyme K144T	Escherichia coli
6.3.2.4	5.4	-	D-Ala	reaction with D-Met + ATP	Escherichia coli
6.3.2.4	6	-	D-Phe	reaction with D-Ala + ATP	Escherichia coli
6.3.2.4	6.4	-	D-Ala	reaction with D-Phe + ATP	Escherichia coli
6.3.2.4	9	-	D-Met	-	Escherichia coli
6.3.2.4	15	-	D-norleucine	reaction with D-Ala + ATP	Escherichia coli
6.3.2.4	20.9	-	D-Ala	C-terminal Ala, mutant enzyme L282R	Escherichia coli
6.3.2.4	22.8	-	D-Ala	C-terminal Ala, mutant enzyme K144A, reaction with 5 mM ATP	Escherichia coli
6.3.2.4	22.9	-	D-Ala	C-terminal Ala, mutant enzyme K144A, reaction with 15 mM ATP	Escherichia coli
6.3.2.4	25.7	-	D-Ala	C-terminal Ala, mutant enzyme Y216F	Escherichia coli
6.3.2.4	33	-	2-aminopentanoate	reaction with D-Ala + ATP	Escherichia coli
6.3.2.4	43.7	-	D-Ala	C-terminal Ala, mutant enzyme E15Q	Escherichia coli
6.3.2.4	57.5	-	D-Ala	C-terminal Ala, mutant enzyme H63Q	Escherichia coli
6.3.2.4	60.4	-	D-Ala	C-terminal Ala, mutant enzyme S150A	Escherichia coli
6.3.2.4	70.3	-	D-Ala	C-terminal Ala, mutant enzyme K144T, reaction with 5 mM ATP	Escherichia coli
6.3.2.4	86	-	D-Ala	C-terminal Ala, mutant enzyme K144T, reaction with 15 mM ATP	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.3.2.4	Escherichia coli	-	wild-type and mutant enzyme forms	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
6.3.2.4	ATP + D-Ala + 2-aminopentanoate	-	Escherichia coli	ADP + phosphate + D-Ala-2-aminopentanoate	-	?
6.3.2.4	ATP + D-Ala + D-Ala	-	Escherichia coli	ADP + phosphate + D-Ala-D-Ala	-	?
6.3.2.4	ATP + D-Ala + D-Met	-	Escherichia coli	ADP + phosphate + D-Ala-D-Met	-	?
6.3.2.4	ATP + D-Ala + D-norleucine	-	Escherichia coli	ADP + phosphate + D-Ala-D-norleucine	-	?
6.3.2.4	ATP + D-Ala + D-Phe	-	Escherichia coli	ADP + phosphate + D-Ala-D-Phe	-	?

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
6.3.2.4	additional information	-	additional information	turnover numbers of wild-type and mutant enzyme forms	Escherichia coli