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Lipoamidase is a multiple hydrolase
1National Children's Medical Research Center, Division of Metabolism, Tokyo, Japan.
The Biochemical Journal
|October 1, 1990
Summary
Lipoamidase, an enzyme from pig brain membranes, hydrolyzes amide, ester, and peptide bonds. Its specificity depends on molecular structure and hydrophobicity, with a high affinity for hydrophobic molecules.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Lipoamidase is a pig brain membrane enzyme.
- Its substrate specificity was previously partially characterized.
Purpose of the Study:
- To extensively study the substrate specificity of purified lipoamidase.
- To elucidate the structural requirements for lipoamidase activity.
Main Methods:
- Purification of lipoamidase from pig brain membrane.
- Enzymatic assays using various substrates like lipoyl 4-aminobenzoate (LPAB), biotinyl 4-aminobenzoate, dipeptides, aspartame, lipoyl esters, lipoyl-lysine, and acetylcholine.
Main Results:
- Lipoamidase hydrolyzes amide, ester, and peptide bonds with stringent structural requirements.
- Specificity is determined by molecular mass and hydrophobicity, favoring longer acyl groups in lipoyl esters.
- While showing some similarities with acetylcholinesterase, lipoamidase exhibits distinct specificity for lipoyl compounds.
Conclusions:
- Lipoamidase recognizes the whole molecular structure of substrates rather than just the bond type.
- The enzyme's role on the brain membrane, particularly its specificity for hydrophobic molecules, requires further investigation.