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Literature summary for 4.1.1.11 extracted from

  • Dusch, N.; Pühler, A.; Kalinowski, J.
    Expression of the Corynebacterium glutamicum panD gene encoding L-aspartate-alpha-decarboxylase leads to pantothenate overproduction in Escherichia coli (1999), Appl. Environ. Microbiol., 65, 1530-1539.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.11

Cloned(Commentary)

Cloned (Comment) Organism
panD gene, overexpression in Corynebacterium glutamicum with 4fold increased enzyme activity and in Escherichia coli with 3fold increased enzyme activity Escherichia coli
panD gene, sequencing, overexpression in Corynebacterium glutamicum with 288fold increased enzyme activity and in Escherichia coli with 41fold increased enzyme activity Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information panD insertion mutant ND2 completely lacks enzyme activity and exhibits beta-alanine auxotrophy Corynebacterium glutamicum
additional information panD mutants Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14100
-
 x * 14100, pi-protein, calculated from the amino acid sequence Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Corynebacterium glutamicum essential for beta-alanine synthesis, involved in pantothenate biosynthesis beta-alanine + CO2
-
 ?
L-aspartate Escherichia coli involved in pantothenate biosynthesis beta-alanine + CO2
-
 ?
L-aspartate Escherichia coli MG1655 involved in pantothenate biosynthesis beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q9X4N0 strain ATCC 13032
-
Escherichia coli P0A790
-
-
Escherichia coli MG1655 P0A790
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism Escherichia coli
proteolytic modification the panD gene product is efficiently proteolytically processed into two subunits, an 11 kDa alpha-subunit and a 2.7 kDa beta-subunit, Gly-24/Ser-25 may be the processing site of the initially translated pi-protein Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Corynebacterium glutamicum beta-alanine + CO2
-
 ?
L-aspartate alpha-decarboxylation Escherichia coli beta-alanine + CO2
-
 ?
L-aspartate essential for beta-alanine synthesis, involved in pantothenate biosynthesis Corynebacterium glutamicum beta-alanine + CO2
-
 ?
L-aspartate involved in pantothenate biosynthesis Escherichia coli beta-alanine + CO2
-
 ?
L-aspartate alpha-decarboxylation Escherichia coli MG1655 beta-alanine + CO2
-
 ?
L-aspartate involved in pantothenate biosynthesis Escherichia coli MG1655 beta-alanine + CO2
-
 ?

Subunits

Subunits Comment Organism
? x * 14100, pi-protein, calculated from the amino acid sequence Corynebacterium glutamicum
tetramer active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein Escherichia coli

Synonyms

Synonyms Comment Organism
PanD
-
 Corynebacterium glutamicum
PanD
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
additional information requires pyruvate as a covalently bound, catalytically active prosthetic group, pyruvoyl-dependent enzyme, the pyruvoyl group is generated at a specific internal serine residue of the inactive pi-protein with the coincident cleavage of the Gly-Ser bond Escherichia coli