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Literature summary for 3.4.24.83 extracted from

  • Goldberg, A.B.; Cho, E.; Miller, C.J.; Lou, H.J.; Turk, B.E.
    Identification of a substrate-selective exosite within the metalloproteinase anthrax lethal factor (2017), J. Biol. Chem., 292, 814-825 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E269A the mutant shows strongly increased cleavage ability for mitogen-activated protein kinase kinase-1 and reduced activity with mitogen-activated protein kinase kinase-6 compared to the wild type enzyme Bacillus anthracis
E539R the mutant shows slightly increased cleavage ability for mitogen-activated protein kinase kinase-1 and reduced activity with mitogen-activated protein kinase kinase-6 compared to the wild type enzyme Bacillus anthracis
K75A the mutant shows wild type activity Bacillus anthracis
L259A the mutant cleaves MEK1 about 2fold less efficiently than the wild type enzyme Bacillus anthracis
L265A the mutation does not significantly impact on MEK1 cleavage Bacillus anthracis
L431A the mutant shows slightly increased cleavage ability for mitogen-activated protein kinase kinase-6 compared to the wild type enzyme Bacillus anthracis
M264A the mutant cleaves MEK1 2.5fold less efficiently than the wild type enzyme Bacillus anthracis
R263A the mutant shows reduced cleavage ability for mitogen-activated protein kinase kinase-1 compared to the wild type enzyme Bacillus anthracis
R491E the mutant cleaves MEK1 about 2fold less efficiently than the wild type enzyme Bacillus anthracis
W271A the mutation completely abolishes cleavage ability of mitogen-activated protein kinase kinase-6 but has no effect on the ability to cleave MEK1. The mutant blocks ERK phosphorylation and growth in a melanoma cell line, suggesting that it may provide a highly selective inhibitor of MEK1/2 for use as a cancer therapeutic Bacillus anthracis
Y268A the mutant cleaves MEK1 6fold less efficiently than the wild type enzyme Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
MEK-1 + H2O Bacillus anthracis
-
?
-
?
MEK-2 + H2O Bacillus anthracis
-
?
-
?
mitogen-activated protein kinase kinase-1 + H2O Bacillus anthracis
-
?
-
?
mitogen-activated protein kinase kinase-3 + H2O Bacillus anthracis
-
?
-
?
mitogen-activated protein kinase kinase-4 + H2O Bacillus anthracis
-
?
-
?
mitogen-activated protein kinase kinase-6 + H2O Bacillus anthracis
-
?
-
?
mitogen-activated protein kinase kinase-7 + H2O Bacillus anthracis
-
?
-
?
NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O Bacillus anthracis
-
?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis P15917
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)acetyl-AKVYPYPME-(2,4-dinitrophenyldiaminopropionic acid) + H2O
-
Bacillus anthracis (7-methoxycoumarin-4-yl)acetyl-AKVYP + YPME-(2,4-dinitrophenyldiaminopropionic acid)
-
?
MEK-1 + H2O
-
Bacillus anthracis ?
-
?
MEK-2 + H2O
-
Bacillus anthracis ?
-
?
mitogen-activated protein kinase kinase-1 + H2O
-
Bacillus anthracis ?
-
?
mitogen-activated protein kinase kinase-3 + H2O
-
Bacillus anthracis ?
-
?
mitogen-activated protein kinase kinase-4 + H2O
-
Bacillus anthracis ?
-
?
mitogen-activated protein kinase kinase-6 + H2O
-
Bacillus anthracis ?
-
?
mitogen-activated protein kinase kinase-7 + H2O
-
Bacillus anthracis ?
-
?
NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O
-
Bacillus anthracis ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 90000, SDS-PAGE Bacillus anthracis