BRENDA - Enzyme Database show

Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase

Schmitzberger, F.; Kilkenny, M.L.; Lobley, C.M.C.; Webb, M.E.; Vinkovic, M.; Matak-Vinkovic, D.; Witty, M.; Chirgadze, D.Y.; Smith, A.G.; Abell, C.; Blundell, T.L.; EMBO J. 22, 6193-6204 (2003)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.1.1.11
overexpression in Escherichia coli
Escherichia coli
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.1.1.11
crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
4.1.1.11
G24S
study of the structure and processing activity
Escherichia coli
4.1.1.11
H11A
study of the structure and processing activity
Escherichia coli
4.1.1.11
additional information
inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity
Escherichia coli
4.1.1.11
S25A
inactive mutant, study of the structure and processing activity
Escherichia coli
4.1.1.11
S25C
study of the structure and processing activity
Escherichia coli
4.1.1.11
S25T
inactive mutant, study of the structure and processing activity
Escherichia coli
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.1.11
14000
-
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.1.1.11
L-aspartate
Escherichia coli
major route of beta-alanine production essential for the biosynthesis of pantothenate
beta-alanine + CO2
-
Escherichia coli
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.1.11
Escherichia coli
P0A790
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
4.1.1.11
proteolytic modification
ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process
Escherichia coli
Purification (Commentary)
EC Number
Commentary
Organism
4.1.1.11
native pro-ADC and mutants
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.11
L-aspartate
Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure
650998
Escherichia coli
beta-alanine + CO2
-
650998
Escherichia coli
?
4.1.1.11
L-aspartate
major route of beta-alanine production essential for the biosynthesis of pantothenate
650998
Escherichia coli
beta-alanine + CO2
-
650998
Escherichia coli
?
Subunits
EC Number
Subunits
Commentary
Organism
4.1.1.11
homotetramer
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
Escherichia coli
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.11
additional information
the translated inactive proenzyme, pi-enzyme, self-processes to create its own covalently bound prosthetic group, a pyruvoyl cofactor, mechanism
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.1.1.11
overexpression in Escherichia coli
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.11
additional information
the translated inactive proenzyme, pi-enzyme, self-processes to create its own covalently bound prosthetic group, a pyruvoyl cofactor, mechanism
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.1.1.11
crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
4.1.1.11
G24S
study of the structure and processing activity
Escherichia coli
4.1.1.11
H11A
study of the structure and processing activity
Escherichia coli
4.1.1.11
additional information
inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity
Escherichia coli
4.1.1.11
S25A
inactive mutant, study of the structure and processing activity
Escherichia coli
4.1.1.11
S25C
study of the structure and processing activity
Escherichia coli
4.1.1.11
S25T
inactive mutant, study of the structure and processing activity
Escherichia coli
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.1.11
14000
-
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.1.1.11
L-aspartate
Escherichia coli
major route of beta-alanine production essential for the biosynthesis of pantothenate
beta-alanine + CO2
-
Escherichia coli
?
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
4.1.1.11
proteolytic modification
ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process
Escherichia coli
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.1.1.11
native pro-ADC and mutants
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.11
L-aspartate
Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure
650998
Escherichia coli
beta-alanine + CO2
-
650998
Escherichia coli
?
4.1.1.11
L-aspartate
major route of beta-alanine production essential for the biosynthesis of pantothenate
650998
Escherichia coli
beta-alanine + CO2
-
650998
Escherichia coli
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.1.1.11
homotetramer
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
Escherichia coli