Any feedback?
Literature summary extracted from
- Expression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD (2002), Protein Expr. Purif., 25, 533-540.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | pharmacology | Mycobacterium tuberculosis is the etiological agent of tuberculosis and PanD is a potential drug target | Mycobacterium tuberculosis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.11 | panD gene, overexpression in Escherichia coli, sequencing | Mycobacterium tuberculosis |
| 4.1.1.12 | expression in Escherichia coli | Mycobacterium tuberculosis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.11 | 0.219 | - |
L-aspartate | pH 7, 37°C, recombinant enzyme | Mycobacterium tuberculosis |  |
| 4.1.1.12 | 0.22 | - |
L-aspartate | 37°C, pH 7.0 | Mycobacterium tuberculosis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.1.1.11 | soluble | recombinant enzyme | Mycobacterium tuberculosis | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 16000 | - |
4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE | Mycobacterium tuberculosis |
| 4.1.1.11 | 64000 | - |
gel filtration | Mycobacterium tuberculosis |
| 4.1.1.12 | 16000 | - |
4 * 16000, SDS-PAGE, PanD is expressed as 16000 Da pro-protein that is processed into 1 alpha and 1 beta subunit | Mycobacterium tuberculosis |
| 4.1.1.12 | 64000 | - |
gel filtration | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.11 | L-aspartate | Mycobacterium tuberculosis | one of the most crucial steps in the pantothenate synthesis pathway | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | Mycobacterium tuberculosis H37Rv | one of the most crucial steps in the pantothenate synthesis pathway | beta-alanine + CO2 | - |
? | |
| 4.1.1.12 | L-aspartate | Mycobacterium tuberculosis | - |
L-alanine + CO2 | - |
? | |
| 4.1.1.12 | L-aspartate | Mycobacterium tuberculosis H37Rv | - |
L-alanine + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.11 | Mycobacterium tuberculosis | - |
- |
- |
| 4.1.1.11 | Mycobacterium tuberculosis H37Rv | - |
- |
- |
| 4.1.1.12 | Mycobacterium tuberculosis | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | proteolytic modification | incubation of panD at 37°C for several hours results in a complete cleavage of the inactive pi-form into the two subunits alpha and beta, optimal cleavage at 37°C for 48 h, cleavage mechanism | Mycobacterium tuberculosis |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.1.11 | recombinant enzyme | Mycobacterium tuberculosis |
| 4.1.1.12 | recombinant panD | Mycobacterium tuberculosis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 2.1 | - |
pH 7, 37°C, recombinant enzyme | Mycobacterium tuberculosis |
| 4.1.1.12 | 2.1 | - |
- |
Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.11 | L-aspartate | - |
Mycobacterium tuberculosis | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | one of the most crucial steps in the pantothenate synthesis pathway | Mycobacterium tuberculosis | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | - |
Mycobacterium tuberculosis H37Rv | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | one of the most crucial steps in the pantothenate synthesis pathway | Mycobacterium tuberculosis H37Rv | beta-alanine + CO2 | - |
? | |
| 4.1.1.12 | L-aspartate | - |
Mycobacterium tuberculosis | L-alanine + CO2 | - |
? | |
| 4.1.1.12 | L-aspartate | - |
Mycobacterium tuberculosis H37Rv | L-alanine + CO2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | tetramer | 4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE | Mycobacterium tuberculosis |
| 4.1.1.12 | tetramer | 4 * 16000, SDS-PAGE, PanD is expressed as 16000 Da pro-protein that is processed into 1 alpha and 1 beta subunit | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | PanD | - |
Mycobacterium tuberculosis |
| 4.1.1.12 | PanD | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 37 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.11 | 0.65 | - |
L-aspartate | pH 7, 37°C, recombinant enzyme | Mycobacterium tuberculosis | |
| 4.1.1.12 | 0.65 | - |
L-aspartate | 37°C, pH 7.0 | Mycobacterium tuberculosis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 7 | - |
assay at | Mycobacterium tuberculosis |
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
