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BRENDA support

Ligand alpha2-Macroglobulin

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Basic Ligand Information

Molecular Formula
BRENDA Name
InChIKey
alpha2-Macroglobulin

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = fragments of alpha2-macroglobulin
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-
alpha2-macroglobulin + H2O = ?
show the reaction diagram
-

Inhibitor in Enzyme-catalyzed Reactions (54 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
association of this protein with LCAT inhibits the activity of LCAT, and may have a role in its catabolism
-
1 unit, 67% inhibition of purified sialyltransferase-1, no inhibition of sialyltransferase-1 activity in microsomes
-
nonspecific proteinase inhibitor
-
38% inhibition by a concentration of 0.001 mM with casein as substrate, and 18% inhibition with succinyl-Ala-Pro-Ala-p-nitroanilide as substrate
-
inhibits alkaline proteolytic activity of purified Arp by 80%
-
may be a physiological inhibitor, 1-3fold molar excess, forms a stable complex with the enzyme
-
weak
-
from human
-
40% inhibition at a 1:1 ratio of cruzipain and alpha2-macroglobulin
-
0.05 mg/ml, 11% inhibition
-
activity towards reduced and carboxymethylated ribonuclease A is significantly inhibited at pH 5.5, the activity towards a peptide substrate, oxidized insulin B-chain, is scarcely inhibited
-
activity with Moloney murrine sarcoma virus-derived gag protein is inhibited at pH 5.5-7.4, activity with B chain of oxidized insulin is scarcely inhibited
-
activity with reduced and carboxymethylated ribonuclease A is significantly inhibited, activity with oxidized insulin B-chain is scarcely inhibited
-
at pH 5.5, RNAse as substrate, at a molar ratio of enzyme/inhibitor of 0.5:1 to 2:1, above a ratio of 2:1 the excess enzyme is not inhibited, structural changes in alpha2-macroglobulin upon complex formation, no inhibition with oxidized insulin B-chain as substrate
-
bovine or Astacus astacus hemolymph, ir
-
a regulatory serpin, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
-
inhibits proteolytic and hemorrhagic activities
-
SDS abolishes inhibition
-

Enzyme Kinetic Parameters

References & Links

Links to other databases for alpha2-Macroglobulin

EXTERNAL LINKS