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Literature summary extracted from

  • Young, C.J.; Richard, K.; Beruar, A.; Lo, S.Y.; Siemann, S.
    An investigation of the pH dependence of copper-substituted anthrax lethal factor and its mechanistic implications (2018), J. Inorg. Biochem., 182, 1-8 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.83 expressed in Bacillus megaterium Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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

EC Number Metals/Ions Comment Organism Structure
3.4.24.83 Cu2+ replacement of Zn2+ by Cu2+ leads to an almost 30fold enhancement of the enzyme activity Bacillus anthracis
3.4.24.83 Zn2+ natural cofactor Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.83 mitogen-activated protein kinase kinase 1 + H2O Bacillus anthracis
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.83 Bacillus anthracis P15917
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.83 acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide + H2O
-
 Bacillus anthracis ?
-
 ?
3.4.24.83 acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
-
 Bacillus anthracis ?
-
 ?
3.4.24.83 MAPKKide + H2O
-
 Bacillus anthracis ?
-
 ?
3.4.24.83 mitogen-activated protein kinase kinase 1 + H2O
-
 Bacillus anthracis ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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
3.4.24.83 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