Literature summary for 4.1.1.11 extracted from

Zhang, T.; Zhang, R.; Xu, M.; Zhang, X.; Yang, T.; Liu, F.; Yang, S.; Rao, Z.
Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production (2018), Process Biochem., 70, 117-123 .

No PubMed abstract available

Search for more literature for 4.1.1.11

Cloned(Commentary)

Cloned (Comment)	Organism
gene panD, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein	Bacillus subtilis
gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein	Corynebacterium glutamicum
gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein	Lactiplantibacillus plantarum

Protein Variants

Protein Variants	Comment	Organism
D41G	site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type	Bacillus subtilis
E56S	site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel	Bacillus subtilis
K63E	site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-aspartate	Corynebacterium glutamicum	-	beta-alanine + CO2	-	?
L-aspartate	Escherichia coli	-	beta-alanine + CO2	-	?
L-aspartate	Bacillus subtilis	-	beta-alanine + CO2	-	?
L-aspartate	Lactiplantibacillus plantarum	-	beta-alanine + CO2	-	?
L-aspartate	Bacillus subtilis 168	-	beta-alanine + CO2	-	?
L-aspartate	Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025	-	beta-alanine + CO2	-	?
L-aspartate	Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1	-	beta-alanine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P52999	-	-
Bacillus subtilis 168	P52999	-	-
Corynebacterium glutamicum	Q9X4N0	-	-
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025	Q9X4N0	-	-
Escherichia coli	P0A790	-	-
Lactiplantibacillus plantarum	Q88Z02	-	-
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1	Q88Z02	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site	Corynebacterium glutamicum
proteolytic modification	bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site	Bacillus subtilis
proteolytic modification	bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site	Lactiplantibacillus plantarum
proteolytic modification	bacterial ADC is usually translated into an inactive zymogen. The zymogen is proteolytically cleaved at the Gly24-Ser25 site. The Escherichia coli ADC requires a Gcn5-like N-acetyltransferase, named PanM (also called PanZ), to help it reach complete maturation	Escherichia coli

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Bacillus subtilis
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Corynebacterium glutamicum
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Lactiplantibacillus plantarum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.5	-	pH 7.0, 37°C, recombinant enzyme	Lactiplantibacillus plantarum
2.4	-	pH 7.0, 37°C, recombinant enzyme	Corynebacterium glutamicum
4.7	-	pH 7.0, 37°C, recombinant enzyme	Bacillus subtilis
5.5	-	pH 7.0, 70°C, recombinant enzyme	Lactiplantibacillus plantarum
9.6	-	pH 7.0, 70°C, recombinant enzyme	Corynebacterium glutamicum
15.7	-	pH 7.0, 65°C, recombinant enzyme	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	-	Corynebacterium glutamicum	beta-alanine + CO2	-	?
L-aspartate	-	Escherichia coli	beta-alanine + CO2	-	?
L-aspartate	-	Bacillus subtilis	beta-alanine + CO2	-	?
L-aspartate	-	Lactiplantibacillus plantarum	beta-alanine + CO2	-	?
L-aspartate	-	Bacillus subtilis 168	beta-alanine + CO2	-	?
L-aspartate	-	Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025	beta-alanine + CO2	-	?
L-aspartate	-	Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1	beta-alanine + CO2	-	?

Subunits

Subunits	Comment	Organism
tetramer	the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit	Corynebacterium glutamicum
tetramer	the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit	Escherichia coli
tetramer	the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit	Bacillus subtilis
tetramer	the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit	Lactiplantibacillus plantarum

Synonyms

Synonyms	Comment	Organism
ADC	-	Corynebacterium glutamicum
ADC	-	Escherichia coli
ADC	-	Bacillus subtilis
ADC	-	Lactiplantibacillus plantarum
BsADC	-	Bacillus subtilis
BsADC	-	Lactiplantibacillus plantarum
CgADC	-	Corynebacterium glutamicum
GcADC	-	Escherichia coli
L-Aspartate alpha-decarboxylase	-	Corynebacterium glutamicum
L-Aspartate alpha-decarboxylase	-	Escherichia coli
L-Aspartate alpha-decarboxylase	-	Bacillus subtilis
L-Aspartate alpha-decarboxylase	-	Lactiplantibacillus plantarum
PanD	-	Corynebacterium glutamicum
PanD	-	Escherichia coli
PanD	-	Bacillus subtilis
PanD	-	Lactiplantibacillus plantarum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	recombinant enzyme	Bacillus subtilis
70	-	recombinant enzyme	Corynebacterium glutamicum
70	-	recombinant enzyme	Lactiplantibacillus plantarum

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
35	90	measured range, activity profile overview	Corynebacterium glutamicum
35	90	measured range, activity profile overview	Bacillus subtilis
35	90	measured range, activity profile overview	Lactiplantibacillus plantarum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	recombinant enzyme	Corynebacterium glutamicum
6.5	-	recombinant enzyme	Lactiplantibacillus plantarum
7	-	recombinant enzyme	Bacillus subtilis

pH Range

pH Minimum	pH Maximum	Comment	Organism
4	11	activity range, profile overview	Corynebacterium glutamicum
4	11	activity range, profile overview	Lactiplantibacillus plantarum
5	10	activity range, profile overview	Bacillus subtilis

pI Value

Organism	Comment	pI Value Maximum	pI Value
Bacillus subtilis	enzyme mutant K63E, sequence calculation	-	5.12
Bacillus subtilis	wild-type enzyme, sequence calculation	-	5.6
Bacillus subtilis	enzyme mutant D41G, sequence calculation	-	5.65
Bacillus subtilis	enzyme mutant E56S, sequence calculation	-	6.09

General Information

General Information	Comment	Organism
evolution	there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor	Corynebacterium glutamicum
evolution	there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor	Escherichia coli
evolution	there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor	Bacillus subtilis
evolution	there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor	Lactiplantibacillus plantarum
malfunction	the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production. The E56S mutant shows an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuated the mechanism-based inactivation of the enzyme	Bacillus subtilis
additional information	structural homology modeling BsADC using the Escherichia coli ADC structure, PDB ID 1PQE, as template	Bacillus subtilis
physiological function	L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid	Corynebacterium glutamicum
physiological function	L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid	Escherichia coli
physiological function	L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid	Bacillus subtilis
physiological function	L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid	Lactiplantibacillus plantarum

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)