Cloned (Comment) | Organism |
---|---|
expressed in Bacillus megaterium | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0016 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
0.0019 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
0.0023 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
0.0042 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | replacement of Zn2+ by Cu2+ leads to an almost 30fold enhancement of the enzyme activity | Bacillus anthracis | |
Zn2+ | natural cofactor | Bacillus anthracis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
mitogen-activated protein kinase kinase 1 + H2O | Bacillus anthracis | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | P15917 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide + H2O | - |
Bacillus anthracis | ? | - |
? | |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O | - |
Bacillus anthracis | ? | - |
? | |
MAPKKide + H2O | - |
Bacillus anthracis | ? | - |
? | |
mitogen-activated protein kinase kinase 1 + H2O | - |
Bacillus anthracis | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.9 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
6.1 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
10.6 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
26.6 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2070 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
3810 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
4660 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis | |
6360 | - |
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide | copper-substituted enzyme, at pH 6.5 and 20°C | Bacillus anthracis |