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Literature summary for 4.1.1.11 extracted from

  • Chopra, S.; Pai, H.; Ranganathan, A.
    Expression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD (2002), Protein Expr. Purif., 25, 533-540.
    View publication on PubMed
Search for more literature for 4.1.1.11

Application

Application Comment Organism
pharmacology Mycobacterium tuberculosis is the etiological agent of tuberculosis and PanD is a potential drug target Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
panD gene, overexpression in Escherichia coli, sequencing Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.219
-
 L-aspartate pH 7, 37°C, recombinant enzyme Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble recombinant enzyme Mycobacterium tuberculosis
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
64000
-
 gel filtration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Mycobacterium tuberculosis one of the most crucial steps in the pantothenate synthesis pathway beta-alanine + CO2
-
 ?
L-aspartate Mycobacterium tuberculosis H37Rv one of the most crucial steps in the pantothenate synthesis pathway beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
recombinant enzyme Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1
-
 pH 7, 37°C, recombinant enzyme Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Mycobacterium tuberculosis beta-alanine + CO2
-
 ?
L-aspartate one of the most crucial steps in the pantothenate synthesis pathway Mycobacterium tuberculosis beta-alanine + CO2
-
 ?
L-aspartate
-
 Mycobacterium tuberculosis H37Rv beta-alanine + CO2
-
 ?
L-aspartate one of the most crucial steps in the pantothenate synthesis pathway Mycobacterium tuberculosis H37Rv beta-alanine + CO2
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
PanD
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.65
-
 L-aspartate pH 7, 37°C, recombinant enzyme Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Mycobacterium tuberculosis