EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    6.3.2.4 | glycine + glycine + ATP |
- |
Synechocystis sp. PCC 6803 |
ADP + Gly-Gly + phosphate |
- |
? |
| 6.3.2.4 | more |
the enzyme is also capable of synthesizing fluorinated dipeptides |
Escherichia coli |
? |
- |
? |
| 6.3.2.4 | more |
DDl is an essential enzyme in bacterial cell wall biosynthesis |
Escherichia coli |
? |
- |
? |
| 6.3.2.4 | more |
no activity with D-Ser, Gly, and D-lactate |
Helicobacter pylori |
? |
- |
? |
| 6.3.2.4 | more |
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 |
? |
- |
? |
| 6.3.2.4 | more |
putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview |
Mycobacterium tuberculosis |
? |
- |
? |
| 6.3.2.4 | more |
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 |
? |
- |
? |
| 6.3.2.4 | more |
putative protein interaction partners of enzyme DdlA from Mycobacterium tuberculosis, overview |
Mycobacterium tuberculosis ATCC 25618 / H37Rv |
? |
- |
? |
