6.3.2.4	ATP + 2 D-Ala	-	Escherichia coli	ADP + phosphate + D-Ala-D-Ala	-	?	408427	
6.3.2.4	ATP + 2 D-Ala	-	Enterococcus faecium	ADP + phosphate + D-Ala-D-Ala	-	?	408427	
6.3.2.4	ATP + 2 D-Ala	-	Leuconostoc mesenteroides	ADP + phosphate + D-Ala-D-Ala	-	?	408427	
6.3.2.4	ATP + 2 D-alanine	-	Escherichia coli	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Leuconostoc mesenteroides	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Mycobacterium tuberculosis	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Acinetobacter baumannii	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Xanthomonas oryzae	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Yersinia pestis	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Thermus thermophilus	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	Y216, S150, and E15 form a hydrogen-bonding triad that orients an omega-loop to close over the active site and also to orient substrate D-Ala1 (the first molecule of substrate that is activated by the enzyme protein). The bifunctional enzyme also catalyzes the formation of D-alanyl-D-lactate (D-alanine-(R)-lactate ligase)	Escherichia coli	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	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	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Mycobacterium tuberculosis ATCC 25618 / H37Rv	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	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	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Mycobacterium tuberculosis H37Rv	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + 2 D-alanine	-	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	ADP + phosphate + D-alanyl-D-alanine	-	?	414296	
6.3.2.4	ATP + Ala + Ala	second enzyme in the three enzyme D-alanine branch of peptidoglycan biosynthesis	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	enzyme involved in peptidoglycan precursor synthesis during sporulation	Lysinibacillus sphaericus	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	a possible cellular role of VanA is to synthesize a modified cell-wall component, with D-Ala-D-Met or D-Ala-Phe instead of D-Ala-D-Ala, which is subsequently not recognized by vancomycin	Escherichia coli	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	the finding that the reactions of EC 6.3.2.4 and EC 6.3.2.10 are reversible may represent a functional regulatory mechanism which determines the level of the lysine-containing UDPMurNAc-pentapeptide depending on the intracellular ATP/ADP ratio	Staphylococcus aureus	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	the finding that the reactions of EC 6.3.2.4 and EC 6.3.2.10 are reversible may represent a functional regulatory mechanism which determines the level of the lysine-containing UDPMurNAc-pentapeptide depending on the intracellular ATP/ADP ratio	Enterococcus faecalis	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	one step in peptidoglycan synthesis: the formation of D-Ala-D-Ala, the terminal dipeptide of the UDP-N-acetylmuramylpentapeptide	Staphylococcus aureus	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	one step in peptidoglycan synthesis: the formation of D-Ala-D-Ala, the terminal dipeptide of the UDP-N-acetylmuramylpentapeptide	Pseudomonas aeruginosa	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	second step in the biosynthesis of bacterial peptidoglycan	Enterococcus faecalis	?	-	?	369333	
6.3.2.4	ATP + Ala + Ala	enzyme involved in peptidoglycan precursor synthesis during sporulation	Lysinibacillus sphaericus 9602	?	-	?	369333	
6.3.2.4	ATP + beta-Ala	at 60°C activity is 1.3% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + ?	-	?	387973	
6.3.2.4	ATP + D-Ala + 2-aminopentanoate	-	Escherichia coli	ADP + phosphate + D-Ala-2-aminopentanoate	-	?	453757	
6.3.2.4	ATP + D-Ala + 2-hydroxybutanoate	-	Enterococcus faecalis	ADP + phosphate + D-Ala-D-2-hydroxybutanoate	-	?	592	
6.3.2.4	ATP + D-Ala + 2-hydroxypentanoate	-	Enterococcus faecalis	ADP + phosphate + D-Ala-D-2-hydroxypentanoate	-	?	593	
6.3.2.4	ATP + D-Ala + D-2-aminopentanoate	-	Escherichia coli	ADP + phosphate + D-Ala-D-2-aminopentanoate	-	?	589	
6.3.2.4	ATP + D-Ala + D-2-aminopentanoate	-	Escherichia coli JM105	ADP + phosphate + D-Ala-D-2-aminopentanoate	-	?	589	
6.3.2.4	ATP + D-Ala + D-Ala	-	Salmonella enterica subsp. enterica serovar Typhimurium	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Bacteria	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Staphylococcus aureus	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Bacillus subtilis	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Escherichia coli	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Pseudomonas aeruginosa	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Enterococcus faecalis	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Streptococcus pyogenes	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Enterococcus faecium	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Thermotoga maritima	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Mycobacterium tuberculosis	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Leuconostoc mesenteroides	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	r	Staphylococcus aureus	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	r	Escherichia coli	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	r	Enterococcus faecalis	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Bacillus subtilis 168	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Enterococcus faecalis R / ATCC 8043	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Escherichia coli JM105	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Mycobacterium tuberculosis H37Rv	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-Ala	-	Thermotoga maritima ATCC 43589	ADP + phosphate + D-Ala-D-Ala	-	?	586	
6.3.2.4	ATP + D-Ala + D-lactate	-	Enterococcus faecalis	ADP + phosphate + D-Ala-D-lactate	-	?	591	
6.3.2.4	ATP + D-Ala + D-lactate	-	Leuconostoc mesenteroides	ADP + phosphate + D-Ala-D-lactate	-	?	591	
6.3.2.4	ATP + D-Ala + D-lactate	-	Leuconostoc mesenteroides	ADP + phosphate + D-Ala-D-lactate	depsipeptide D-Ala-D-lactate is responsible for the intrinsic resistance of Leuconostoc mesenteroides to vancomycin	?	591	
6.3.2.4	ATP + D-Ala + D-lactate	enzyme uses both D-Ala and D-lactate as a substrate	Enterococcus faecium	ADP + phosphate + D-Ala-D-lactate	-	?	591	
6.3.2.4	ATP + D-Ala + D-lactate	D-lactate is not a substrate for wild-type, but for mutants S137A/Y207F, S137F/Y207F, S137T/Y207F, S137G/Y207F, Y207F	Thermotoga maritima	ADP + phosphate + D-Ala-D-lactate	-	?	591	
6.3.2.4	ATP + D-Ala + D-lactate	D-lactate is not a substrate for wild-type, but for mutants S137A/Y207F, S137F/Y207F, S137T/Y207F, S137G/Y207F, Y207F	Thermotoga maritima ATCC 43589	ADP + phosphate + D-Ala-D-lactate	-	?	591	
6.3.2.4	ATP + D-Ala + D-Met	-	Escherichia coli	ADP + phosphate + D-Ala-D-Met	-	?	587	
6.3.2.4	ATP + D-Ala + D-Met	-	Escherichia coli JM105	ADP + phosphate + D-Ala-D-Met	-	?	587	
6.3.2.4	ATP + D-Ala + D-norleucine	-	Escherichia coli	ADP + phosphate + D-Ala-D-norleucine	-	?	590	
6.3.2.4	ATP + D-Ala + D-norleucine	-	Escherichia coli JM105	ADP + phosphate + D-Ala-D-norleucine	-	?	590	
6.3.2.4	ATP + D-Ala + D-Phe	-	Escherichia coli	ADP + phosphate + D-Ala-D-Phe	-	?	588	
6.3.2.4	ATP + D-Ala + D-Phe	-	Escherichia coli JM105	ADP + phosphate + D-Ala-D-Phe	-	?	588	
6.3.2.4	ATP + D-Ala + NH3	the D-AlaNH2 production of enzyme S293X mutants is optimized, the S293E variant, which is selected as the best enzyme for D-AlaNH2 production, exhibits an optimal activity at pH 9.0 and 40°C for D-AlaNH2 production. The S293E variant catalyzes the synthesis of 9.3 and 35.7 mM of D-AlaNH2 from 10 and 50 mM D-Ala and 3 M NH4Cl with conversion yields of 93% and 71.4%, respectively. The S293E variant exhibits higher reaction specificity to D-AlaNH2 production compared with the S293D variant and the other variants	Thermus thermophilus	ADP + phosphate + D-AlaNH2	-	?	443126	
6.3.2.4	ATP + D-Ala + NH3	the D-AlaNH2 production of enzyme S293X mutants is optimized, the S293E variant, which is selected as the best enzyme for D-AlaNH2 production, exhibits an optimal activity at pH 9.0 and 40°C for D-AlaNH2 production. The S293E variant catalyzes the synthesis of 9.3 and 35.7 mM of D-AlaNH2 from 10 and 50 mM D-Ala and 3 M NH4Cl with conversion yields of 93% and 71.4%, respectively. The S293E variant exhibits higher reaction specificity to D-AlaNH2 production compared with the S293D variant and the other variants	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	ADP + phosphate + D-AlaNH2	-	?	443126	
6.3.2.4	ATP + D-alanine	-	Chlamydia trachomatis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Escherichia coli	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Enterococcus faecalis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Enterococcus faecium	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Mycobacterium tuberculosis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Helicobacter pylori	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Thermotoga maritima	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Streptomyces lavendulae	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Synechocystis sp. PCC 6803	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Oceanobacillus iheyensis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Staphylococcus aureus	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Mycolicibacterium smegmatis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	essential enzyme	Enterococcus faecalis	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	D-alanine:D-alanine ligase is an essential enzyme in bacterial cell wall biosynthesis and an important target for developing new antibiotics	Staphylococcus aureus	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	the enzyme shows relatively weak binding affinity and poor catalytic activity against the substrate D-Ala in vitro, active site structure, overview	Helicobacter pylori	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Oceanobacillus iheyensis JCM 11309	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Streptomyces lavendulae ATCC 25233	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine	-	Enterococcus faecium BM4416	ADP + phosphate + D-alanyl-D-alanine	-	?	369131	
6.3.2.4	ATP + D-alanine + D-serine	-	Escherichia coli	ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine	-	?	379287	
6.3.2.4	ATP + D-alanine + D-serine	-	Thermotoga maritima	ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine	-	?	379287	
6.3.2.4	ATP + D-alanine + D-serine	-	Synechocystis sp. PCC 6803	ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine	-	?	379287	
6.3.2.4	ATP + D-Arg	at 60°C activity is 0.43% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Arg-D-Arg	-	?	387995	
6.3.2.4	ATP + D-Asn	at 60°C activity is 0.22% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Asn-D-Asn	-	?	387996	
6.3.2.4	ATP + D-Asp	at 60°C activity is 0.051% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Asp-D-Asp	-	?	387998	
6.3.2.4	ATP + D-Cys	at 60°C activity is 29% of the activity with D-Ala	Thermotoga maritima	ADP + phosphate + D-Cys-D-Cys	-	?	388001	
6.3.2.4	ATP + D-Gln	at 60°C activity is 0.56% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Gln-D-Gln	-	?	388010	
6.3.2.4	ATP + D-Glu	at 60°C activity is 0.012% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Glu-D-Glu	-	?	388012	
6.3.2.4	ATP + D-His	at 60°C activity is 0.49% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-His-D-His	-	?	388013	
6.3.2.4	ATP + D-Ile	at 60°C activity is 0.36% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Ile-D-Ile	-	?	388014	
6.3.2.4	ATP + D-Leu	at 60°C activity is 0.31% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Leu-D-Leu	-	?	388015	
6.3.2.4	ATP + D-Lys	at 60°C activity is 0.6% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Lys-D-Lys	-	?	388016	
6.3.2.4	ATP + D-Met	at 60°C activity is 0.34% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Met-D-Met	-	?	388017	
6.3.2.4	ATP + D-Phe	at 60°C activity is 0.31% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Phe-D-Phe	-	?	388019	
6.3.2.4	ATP + D-Pro	at 60°C activity is 0.29% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Pro-D-Pro	-	?	388020	
6.3.2.4	ATP + D-Ser	at 60°C activity is 16% of the activity with D-Ala	Thermotoga maritima	ADP + phosphate + D-Ser-D-Ser	-	?	388021	
6.3.2.4	ATP + D-serine	-	Escherichia coli	ADP + phosphate + D-alanyl-D-serine	-	?	369132	
6.3.2.4	ATP + D-Thr	at 60°C activity is 2.2% of the activity with D-Ala	Thermotoga maritima	ADP + phosphate + D-Thr-D-Thr	-	?	388022	
6.3.2.4	ATP + D-Trp	at 60°C activity is 0.1% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Trp-D-Trp	-	?	388023	
6.3.2.4	ATP + D-Val	at 60°C activity is 0.43% of the activity with D-Ala, no activity at 37°C	Thermotoga maritima	ADP + phosphate + D-Val-D-Val	-	?	388025	
6.3.2.4	ATP + Gly	at 60°C activity is 3.6% of the activity with D-Ala	Thermotoga maritima	ADP + phosphate + Gly-Gly	-	?	388049	
6.3.2.4	beta-alanine + beta-alanine + ATP	-	Thermotoga maritima	beta-alanyl-beta-alanine + ADP + phosphate	1.3% of the activity with D-serine	?	411741	
6.3.2.4	D-alanine + D-alanine + ATP	-	Thermotoga maritima	D-alanyl-D-alanine + ADP + phosphate	-	?	411926	
6.3.2.4	D-cycloserine	-	Chlamydia trachomatis	?	-	?	379648	
6.3.2.4	D-cycloserine	-	Streptomyces lavendulae	?	-	?	379648	
6.3.2.4	D-cycloserine	-	Streptomyces lavendulae ATCC 25233	?	-	?	379648	
6.3.2.4	D-cysteine + ATP	-	Escherichia coli	ADP + D-cysteinyl-D-cysteine	-	?	379649	
6.3.2.4	D-cysteine + ATP	-	Thermotoga maritima	ADP + D-cysteinyl-D-cysteine	-	?	379649	
6.3.2.4	D-cysteine + ATP	-	Synechocystis sp. PCC 6803	ADP + D-cysteinyl-D-cysteine	-	?	379649	
6.3.2.4	D-cysteine + D-cysteine + ATP	-	Thermotoga maritima	D-cysteinyl-D-cysteine + ADP + phosphate	29% of the activity with D-serine	?	411937	
6.3.2.4	D-serine + ATP	-	Escherichia coli	ADP + D-serinyl-D-serine	-	?	379676	
6.3.2.4	D-serine + ATP	-	Thermotoga maritima	ADP + D-serinyl-D-serine	-	?	379676	
6.3.2.4	D-serine + ATP	-	Synechocystis sp. PCC 6803	ADP + D-serinyl-D-serine	-	?	379676	
6.3.2.4	D-serine + D-serine + ATP	-	Thermotoga maritima	D-seryl-D-serine + ADP + phosphate	16% of the activity with D-serine	?	411949	
6.3.2.4	D-threonine + ATP	-	Escherichia coli	ADP + D-threonyl-D-threonine	-	?	379679	
6.3.2.4	D-threonine + ATP	-	Thermotoga maritima	ADP + D-threonyl-D-threonine	-	?	379679	
6.3.2.4	D-threonine + ATP	-	Synechocystis sp. PCC 6803	ADP + D-threonyl-D-threonine	-	?	379679	
6.3.2.4	D-threonine + D-threonine + ATP	-	Thermotoga maritima	D-threonyl-D-threonine + ADP + phosphate	2.2% of the activity with D-serine	?	411950	
6.3.2.4	dipeptides + ATP	-	Escherichia coli	?	-	?	379700	
6.3.2.4	dipeptides + ATP	-	Thermotoga maritima	?	-	?	379700	
6.3.2.4	dipeptides + ATP	-	Synechocystis sp. PCC 6803	?	-	?	379700	
6.3.2.4	dipeptides + ATP	-	Oceanobacillus iheyensis	?	-	?	379700	
6.3.2.4	dipeptides + ATP	-	Oceanobacillus iheyensis JCM 11309	?	-	?	379700	
6.3.2.4	glycine + D-alanine + ATP	-	Thermotoga maritima	glycyl-D-alanine + ADP + phosphate	3.6% of the activity with D-serine	?	412109	
6.3.2.4	glycine + glycine + ATP	-	Escherichia coli	ADP + Gly-Gly + phosphate	-	?	379810	
6.3.2.4	glycine + glycine + ATP	-	Thermotoga maritima	ADP + Gly-Gly + phosphate	-	?	379810	
6.3.2.4	glycine + glycine + ATP	-	Synechocystis sp. PCC 6803	ADP + Gly-Gly + phosphate	-	?	379810	
6.3.2.4	additional information	the enzyme is also capable of synthesizing fluorinated dipeptides	Escherichia coli	?	-	?	89	
6.3.2.4	additional information	DDl is an essential enzyme in bacterial cell wall biosynthesis	Escherichia coli	?	-	?	89	
6.3.2.4	additional information	no activity with D-Ser, Gly, and D-lactate	Helicobacter pylori	?	-	?	89	
6.3.2.4	additional information	substrate specificity expands at high temperature. At 37°C, enzyme shows reactivity only for D-alanine, D-serine, D-threonine, D-cysteine and glycine. At 60°C, substrates additionally include D-lysine, D-glutamine, D-histidine, D-arginine, D-valine, D-isoleucine, D-methionine, D-leucine, D-phenylalanine, D-proline, and D-asparagine, all below 1% of the activity with D-alanine	Thermotoga maritima	?	-	?	89	
6.3.2.4	additional information	putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview	Mycobacterium tuberculosis	?	-	?	89	
6.3.2.4	additional information	substrate-binding mechanism of enzyme YpDDL involving conformational changes of the loops, overview. Two D-alanine-binding sites are located next to each other between the N-terminal domain and the C-terminal domain, and an ATP-binding site exists between the central and the C-terminal domains	Yersinia pestis	?	-	?	89	
6.3.2.4	additional information	putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview	Mycobacterium tuberculosis ATCC 25618 / H37Rv	?	-	?	89