Any feedback?
Literature summary for 4.1.1.1 extracted from
- Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity (2002), Biochemistry, 41, 6164-6169.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D28A | active site mutant with very low activity | Saccharomyces cerevisiae |
| D28N | active site mutant with very low activity | Saccharomyces cerevisiae |
| E477Q | active site mutant with very low activity | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | cofactor, requirement | Saccharomyces cerevisiae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Saccharomyces cerevisiae | - |
acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type and D28A, D28N, E477Q mutant YPDC | Saccharomyces cerevisiae |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | not: pyruvamide | Saccharomyces cerevisiae | ? | - |
? | |
| pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
| pyruvate | alternating sites mechanism | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | dimer of dimers, minimal catalytic unit is a functional dimer, two active sites in the functional dimer act in an antiphase manner during the reaction, with each active site eventually completing the full catalytic cycle, study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| YPDC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | requirement | Saccharomyces cerevisiae | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
