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beta-chloro-L-Ala + H2O
pyruvate + Cl- + NH4+
-
-
-
?
erythro-beta-hydroxy-DL-Asp
?
Pseudomonas dacunhae
-
the reaction of erythro-beta-hydroxy-DL-Asp with ABDC is at least 16700fold slower than that with L-aspartate
-
-
?
erythro-beta-Hydroxyaspartate
L-Ser + CO2
-
-
-
?
L-Asp
?
-
in coordination with pyruvate carboxylase, aspartate 4-decarboxylase is important in regulating the metabolic fate of oxaloacetate and thus plays a role in determining the efficiency of carbohydrate metabolism
-
-
?
L-aspartate
beta-alanine + CO2
-
more than 95% of the substrate is converted to beta-alanine during a 20 min incubation period
-
-
?
L-aspartate
L-alanine + CO2
L-aspartic acid
L-alanine + CO2
Pseudomonas dacunhae
-
-
-
-
?
L-Cysteinesulfinate
L-Ala + SO2
succinate
?
Pseudomonas dacunhae
-
-
-
-
?
threo-beta-hydroxy-DL-Asp
?
Pseudomonas dacunhae
-
the reaction of threo-beta-hydroxy-DL-Asp with ABDC is at least 1000fold slower than that with L-aspartate
-
-
?
threo-beta-Hydroxyaspartate
L-Ser + CO2
-
-
-
?
additional information
?
-
Aminomalonate
Gly + CO2
-
-
-
?
Aminomalonate
Gly + CO2
-
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
replacement of the beta-carboxyl group of Asp by hydrogen occurs in an inversion mode
-
?
L-Asp
L-Ala + CO2
-
highly specific for L-Asp
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
highly specific for L-Asp
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
highly specific for L-Asp
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomonas dacunhae
-
highly specific for L-Asp
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
-
?
L-Asp
L-Ala + CO2
Pseudomycobacteria
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-Asp
L-Ala + CO2
-
-
-
?
L-aspartate
L-alanine + CO2
-
-
?
L-aspartate
L-alanine + CO2
-
-
-
?
L-aspartate
L-alanine + CO2
-
-
-
?
L-aspartate
L-alanine + CO2
Pseudomonas dacunhae
-
-
-
-
?
L-aspartate
L-alanine + CO2
-
-
-
?
L-aspartate
L-alanine + CO2
-
-
-
-
?
L-aspartate
L-alanine + CO2
the decarboxylation activity is 2477fold higher than the aminotransferase activity of the enzyme, highly preferred substrate
-
-
?
L-Cysteinesulfinate
L-Ala + SO2
-
-
-
?
L-Cysteinesulfinate
L-Ala + SO2
Pseudomonas dacunhae
-
-
-
-
?
L-Cysteinesulfinate
L-Ala + SO2
-
-
-
-
?
additional information
?
-
-
no activity with L-glutamate
-
-
?
additional information
?
-
-
also catalyzes transamination between 2-oxoglutarate and L-Asp, L-Ala, L-Met, L-Phe, L-Glu, L-Val, L-Leu, L-Ser or L-glutathione
-
-
?
additional information
?
-
-
transamination between L-Asp and pyruvate
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
additional information
?
-
Pseudomonas dacunhae
-
-
-
-
?
additional information
?
-
Pseudomonas dacunhae
-
transamination between Asp and 2-oxoglutarate
-
-
?
additional information
?
-
Asd is a bifunctional enzyme performing decarboxylation and aminotransferase activities on L-aspartate
-
-
?
additional information
?
-
D-aspartate, L-lysine, L-asparagine, L-glutamate, and L-glutamine are poor substrates in beta-elimination and transamination reaction catalyzes by the enzyme, substrate specificity, overview
-
-
?
additional information
?
-
-
D-aspartate, L-lysine, L-asparagine, L-glutamate, and L-glutamine are poor substrates in beta-elimination and transamination reaction catalyzes by the enzyme, substrate specificity, overview
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
additional information
?
-
-
no inherent transaminase activity
-
-
?
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E84K/E88K
the mutant retains 13% activity compared to the wild type enzyme
K17A
the mutant shows 131.2% activity compared to the wild type enzyme
K315A
the mutant shows 36.7% activity compared to the wild type enzyme
R37A
the mutant shows 10.4% activity compared to the wild type enzyme
R425A
the mutant retains 2.5% activity compared to the wild type enzyme
R487A
completely inactive mutant
S67A/Y68A/M69A
the mutant retains less than 1% activity compared to the wild type enzyme
S67E/Y68E/M69E
the mutations produce an inactive dimer
S67R/Y68R/M69R
the mutations produce an inactive dimer
Y134F
the mutant shows 40.3% activity compared to the wild type enzyme
Y207F
the mutant shows 10.7% activity compared to the wild type enzyme
Y441F
the mutant shows 40.8% activity compared to the wild type enzyme
K17A
-
the mutant shows 131.2% activity compared to the wild type enzyme
-
K315A
-
the mutant shows 36.7% activity compared to the wild type enzyme
-
R37A
-
the mutant shows 10.4% activity compared to the wild type enzyme
-
R425A
-
the mutant retains 2.5% activity compared to the wild type enzyme
-
R487A
-
completely inactive mutant
-
S298R
Pseudomonas dacunhae
the mutant shows very low activity
D360P
site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme
F204W
site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but highly increased aminotransferase compared to the wild-type enzyme
H123Y
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity and slightly increased aminotransferase compared to the wild-type enzyme
H337R
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but similar aminotransferase compared to the wild-type enzyme
K347R
site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme
M178L
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme
P257H
-
the mutation results in inactivation of the enzyme, but does not affect the overall structure (0.08% of the wild type enzymatic activity)
S298R
-
the mutation disassembles the dodecameric L-aspartate 4-decarboxylase into inactive dimers (0.1% of the wild type enzymatic activity)
V475L
site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme
Y207H
-
the mutation results in inactivation of the enzyme, but does not affect the overall structure (0.08% of the wild type enzymatic activity)
R37A
Pseudomonas dacunhae
the mutant shows reduced activity
R37A
Pseudomonas dacunhae
-
the mutant shows a 5000fold slower kcat value than the wild type enzyme
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Wilson, E.M.; Kornberg, H.L.
Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp.
Biochem. J.
88
578-587
1963
Achromobacter sp.
brenda
Palekar, A.G.; Tate, S.S.; Meister, A.
Inhibition of aspartate beta-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine
Biochemistry
9
2310-2315
1970
Alcaligenes faecalis
brenda
Novogrodsky, A.; Meister, A.
Control of aspartate beta-decarboxylase activity by transamination
J. Biol. Chem.
239
879-888
1964
Alcaligenes faecalis
brenda
Kakimoto, T.; Kato, J.; Shibatani, T.; Nishimura, N.; Chibata, I.
Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae
J. Biol. Chem.
244
353-358
1969
Pseudomonas dacunhae
brenda
Tate, S.S.; Meister, A.
L-Aspartate-beta-decarboxylase. Structure, catalytic activities, and allosteric regulation
Adv. Enzymol. Relat. Areas Mol. Biol.
35
503-543
1971
Acetobacter sp., Achromobacter sp., Alcaligenes faecalis, Bombyx mori, Clostridium perfringens, Astacoidea, Desulfovibrio desulfuricans, Lobster, Nocardia globerula, Pseudomonas dacunhae, Pseudomycobacteria
brenda
Relyea, N.M.; Tate, S.S.; Meister, A.
Affinity labeling of the active center of L-aspartate-beta-decarboxylase with beta-chloro-L-alanine
J. Biol. Chem.
249
1519-1524
1974
Alcaligenes faecalis
brenda
Ikeda, S.; Fukui, S.
Studies of the activity of subunits of aspartate 4-decarboxylase immobilized on Sepharose
Eur. J. Biochem.
46
553-558
1974
Pseudomonas dacunhae
brenda
Shibatani, T.; Kakimoto, T.; Kato, J.; Nishimura, N.; Chibata, I.
Properties of crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae
J. Ferment. Technol.
52
886-898
1974
Pseudomonas dacunhae
-
brenda
Takamatsu, S.; Yamamoto, K.; Tosa, T.; Chibata, I.
Stabilization of L-aspartate beta-decarboxylase activity of Pseudomonas dacunhae immobilized with carrageenan
J. Ferment. Technol.
59
489-493
1981
Pseudomonas dacunhae
-
brenda
Rathod, P.K.; Fellman, J.H.
Regulation of mammalian aspartate-4-decarboxylase: its possible role in oxaloacetate and energy metabolism
Arch. Biochem. Biophys.
238
447-451
1985
Rattus norvegicus
brenda
Wong, P.T.H.
Rat brain aspartate beta-decarboxylase. A comparative study with the liver enzyme
Neurochem. Int.
7
351-355
1985
Rattus norvegicus
brenda
Rathod, P.K.; Fellman, J.H.
Identification of mammalian aspartate-4-decarboxylase
Arch. Biochem. Biophys.
238
435-446
1985
Bos taurus, Gallus gallus, Felis catus, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Takamatsu, S.; Ryu, D.D.Y
Recirculating bioreactor-separator system for simultaneous biotransformation and recovery of product: immobilized L-aspartate beta-decarboxylase reactor system
Biotechnol. Bioeng.
32
184-191
1988
Pseudomonas dacunhae
brenda
Abelian, V.A.; Bagdasarian, S.N.; Afrikian, E.G.
Intracellular L-aspartate-beta-decarboxylase of Pseudomonas sp. and Alcaligenes sp. and its immobilization
Biokhimiya
56
1288-1295
1991
Alcaligenes sp., Pseudomonas sp.
brenda
El-Rahmany, T.A.
Comparison of L-aspartate 4-carboxy-lyases of Cunninghammela elegans and Penicillium citrinum
Microbiol. Res.
149
253-157
1994
Cunninghamella elegans, Penicillium citrinum
brenda
Rosenberg, R.M.; O'Leary, M.H.
Aspartate beta-decarboxylase from Alcaligenes: carbon-13 kinetic isotope effect and deuterium exchange experiments
Biochemistry
24
1598-1603
1985
Alcaligenes faecalis
brenda
Chang, C.C.; Laghai, A.; O'Leary, M.H.; Floss, H.G.
Some stereochemical features of aspartate beta-decarboxylase
J. Biol. Chem.
257
3564-3569
1982
Alcaligenes faecalis
brenda
Chen, C.C.; Chou, T.L.; Lee, C.Y.
Cloning, expression and characterization of L-aspartate beta-decarboxylase gene from Alcaligenes faecalis CCRC 11585
J. Ind. Microbiol. Biotechnol.
25
132-140
2000
Comamonas testosteroni (Q93QX0)
-
brenda
Chopra, S.; Pai, H.; Ranganathan, A.
Expression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD
Protein Expr. Purif.
25
533-540
2002
Mycobacterium tuberculosis
brenda
Furui, M.; Yamashita, K.
Pressurized reaction method for continuous production of L-alanine by immobilized Pseudomonas dacunhae cells
J. Ferment. Technol.
61
587-591
1983
Pseudomonas dacunhae
-
brenda
Wang, N.C.; Lee, C.Y.
Enhanced transaminase activity of a bifunctional L-aspartate 4-decarboxylase
Biochem. Biophys. Res. Commun.
356
368-373
2007
Pseudomonas sp. (Q53IZ1)
brenda
Wang, N.C.; Lee, C.Y.
Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas sp. ATCC 19121 and characterization of the bifunctional recombinant enzyme
Appl. Microbiol. Biotechnol.
73
339-348
2006
Pseudomonas sp. (Q53IZ1), Pseudomonas sp.
brenda
Wang, N.C.; Ko, T.P.; Lee, C.Y.
Inactive S298R disassembles the dodecameric L-aspartate 4-decarboxylase into dimers
Biochem. Biophys. Res. Commun.
374
134-137
2008
Pseudomonas sp.
brenda
Lima, S.; Sundararaju, B.; Huang, C.; Khristoforov, R.; Momany, C.; Phillips, R.S.
The crystal structure of the Pseudomonas dacunhae aspartate-beta-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5-phosphate-dependent enzyme
J. Mol. Biol.
388
98-108
2009
Pseudomonas dacunhae (Q845W8)
brenda
Richardson, G.; Ding, H.; Rocheleau, T.; Mayhew, G.; Reddy, E.; Han, Q.; Christensen, B.M.; Li, J.
An examination of aspartate decarboxylase and glutamate decarboxylase activity in mosquitoes
Mol. Biol. Rep.
37
3199-3205
2009
Aedes aegypti
brenda
Chen, H.J.; Ko, T.P.; Lee, C.Y.; Wang, N.C.; Wang, A.H.
Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase
Structure
17
517-529
2009
Pseudomonas sp., Comamonas testosteroni (Q93QX0), Comamonas testosteroni CCRC 11585 (Q93QX0)
brenda
Phillips, R.S.; Lima, S.; Khristoforov, R.; Sudararaju, B.
Insights into the mechanism of Pseudomonas dacunhae aspartate beta-decarboxylase from rapid-scanning stopped-flow kinetics
Biochemistry
49
5066-5073
2010
Pseudomonas dacunhae
brenda