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Literature summary for 3.4.23.46 extracted from
- Crystal structure of an active form of BACE1: an enzyme responsible for amyloid {beta} protein production (2008), Mol. Cell. Biol., 28, 3663-3671.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of the active form of BACE1, dehydrated form characterized, enzyme-inhibitor complex analyzed | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| OM99-2 | pH dependence of BACE1 activity in solution with and without OM99-2 shown, surface representation in the active site cleft with superimposed OM99-2 at pH 5 shown by crystallization, active and inactive structures determined | Homo sapiens |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endosome | cycling of BACE1 between the cell surface and the endosomal system, activation of BACE1 interconvertible during cellular trafficking | Homo sapiens | 5768 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P56817 | - |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
structural features of the active form of BACE1 described, regulatory mechanism of enzymatic activity of BACE1 characterized by crystallization, conformation of the flap and subsites that promote substrate binding determined, functionally essential residues and water molecules for key role in the iterative activation of BACE1 shown, dependence of BACE1 activity on dynamics of a catalytically required aspartic acid-bound water molecule BACE1 shown, data refinement and statistics summarized | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | report on crystal structure of the catalytically active form of BACE1, novel structural features of the active form of BACE1 determined, mechanism of modulation of BACE1 activity during cellular trafficking shown by crystallization | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BACE1 | - |
Homo sapiens |
| beta-secretase | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
activity assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
pH dependence of BACE1 activity in solution shown | Homo sapiens |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 7 | different pH conditions used for studies on crystallization of BACE1 | Homo sapiens |
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Release 2023.1 (January 2023)
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