Information on EC 4.1.1.64 - 2,2-Dialkylglycine decarboxylase (pyruvate):
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EC NUMBERCOMMENTARY
4.1.1.64-

RECOMMENDED NAMEGeneOntology No.
2,2-Dialkylglycine decarboxylase (pyruvate)GO:0047432

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		----
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		cooperativity does not play a role in catalysis or regulationBurkholderia cepacia-4753
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		model in which the interaction between a carboxylate group in the B subsite and Arg406 is a prerequisite to proton donation to and removal from CalphaBurkholderia cepacia-4754
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		the reaction of the slower substrates L-phenylglycine and 1-aminocyclohexane-1-carboxylate may have external aldimine formation as the rate-determining step. The biphasic reactions of 2-methyl-2-aminomalonate, 1-aminocyclopentane-1-carboxylate, isopropylamine and Gly all have external aldimine formation as the rapid observable stepBurkholderia cepacia-4755
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		mechanism; pH-studies on the mechanismBurkholderia cepacia-4756
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		kinetics, a rate-limiting, concerted Calpha-decarboxylation/c4’-protonation mechanism for the AIB decarboxylation reaction and rapid equilibrium quinoid formation followed by rate-limiting protonation to the ketimine intermediate for the L-alanine transamination half-reactionBurkholderia cepacia-650033
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		kinetics of inhibitionBurkholderia cepacia-650109
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
show the reaction diagram		mechanismBurkholderia cepacia-652809

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
decarboxylation----
transaminationBurkholderia cepacia--661129

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
2,2-dialkylglycine carboxy-lyase (amino-transferring; L-alanine-forming)A pyridoxal-phosphate protein. Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
2,2-Dialkyl-2-amino acid-pyruvate aminotransferase----
alpha-Dialkyl amino acid transaminase----
alpha-Dialkylamino acid aminotransferase----
alpha-Dialkylamino acid transaminase----
Decarboxylase, dialkyl amino acid (pyruvate)----
DGD----
DGDBurkholderia cepacia--664227
Dialkylamino-acid decarboxylase (pyruvate)----
dialkylglycine decarboxylaseBurkholderia cepacia--664227
L-Alanine-alpha-ketobutyrate aminotransferase----

CAS REGISTRY NUMBERCOMMENTARY
9032-17-1-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aspergillus candidusIFO 43894757--Manually annotated by BRENDA team
Aspergillus oryzaeIFO 41764757--Manually annotated by BRENDA team
Aspergillus parasiticusIFO 4301, AHU 7165, IAM 25514757--Manually annotated by BRENDA team
Aspergillus sojaeIFO 4274, low activity4757--Manually annotated by BRENDA team
Burkholderia cepacia-4749, 4750, 4752, 4753, 4754, 4755, 4756, 4759, 650033, 661129, 664227--Manually annotated by BRENDA team
Burkholderia cepacia-4758, 650109, 652809, 661182P16932UniprotManually annotated by BRENDA team
Fusarium merismoideslow activity4757--Manually annotated by BRENDA team
Fusarium solani-4757--Manually annotated by BRENDA team
Mucor globosusIFO 6745, low activity4757--Manually annotated by BRENDA team
Mycosphaerella graminicolawheat blotch fungus650912Q7Z8J1SwissProtManually annotated by BRENDA team
Pseudomonas sp.-4748, 4751--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
1-Amino-1-cyclohexane-carboxylate + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
1-Amino-1-cyclopentane-carboxylate + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
2-Aminoisobutanoate + 2-oxobutanoateAcetone + ? + CO2
show the reaction diagram		Fusarium solani--4757---
2-Aminoisobutanoate + 2-oxoisopentanoateAcetone + ? + CO2
show the reaction diagram		Fusarium solani--4757---
2-Aminoisobutanoate + 2-oxopentanoateAcetone + ? + CO2
show the reaction diagram		Fusarium solani--4757---
2-Aminoisobutanoate + glyoxylateAcetone + ? + CO2
show the reaction diagram		Fusarium solani--4757---
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--4749---
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--4750-4750-
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--4754---
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--661129, 661182--?
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Aspergillus oryzae, Fusarium solani, Aspergillus parasiticus, Aspergillus candidus, Mucor globosus, Aspergillus sojae, Fusarium merismoides--4757---
2-Aminoisobutanoate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Pseudomonas sp.-reverse of decarboxylationin is not deteced, exchange transamination between L-Ala and pyruvate is reversible4751-4751-
2-aminoisobutyrate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--4756-4756?
2-aminoisobutyrate + pyruvateL-Ala + acetone + CO2
show the reaction diagram		Burkholderia cepacia--664227--?
2-Oxobutanoate + DL-homocysteine?
show the reaction diagram		Pseudomonas sp.-weak activity4748---
2-Oxobutanoate + DL-Ile?
show the reaction diagram		Pseudomonas sp.--4751---
2-Oxobutanoate + L-2-aminobutanoate?
show the reaction diagram		Pseudomonas sp.--4748---
2-Oxobutanoate + L-Ala?
show the reaction diagram		Pseudomonas sp.--4748, 4751---
2-Oxobutanoate + L-citrulline?
show the reaction diagram		Pseudomonas sp.-weak activity4748---
2-Oxobutanoate + L-Cys?
show the reaction diagram		Pseudomonas sp.-weak activity4748---
2-Oxobutanoate + L-Leu?
show the reaction diagram		Pseudomonas sp.-weak activity4748---
2-Oxobutanoate + L-Met?
show the reaction diagram		Pseudomonas sp.-weak activity4748---
2-Oxobutanoate + L-norleucine?
show the reaction diagram		Pseudomonas sp.--4748---
2-Oxobutanoate + L-norvaline?
show the reaction diagram		Pseudomonas sp.--4748---
2-Oxobutanoate + S-methyl-L-Cys?
show the reaction diagram		Pseudomonas sp.--4748---
2-Oxohexanoate + DL-Ile?
show the reaction diagram		Pseudomonas sp.--4751---
2-Oxohexanoate + L-Ala?
show the reaction diagram		Pseudomonas sp.--4751---
2-Oxohexanoate + L-Ala?
show the reaction diagram		Pseudomonas sp.-81% of the activity with 2-oxobutanoate4748---
2-Oxopentanoate + DL-Ile?
show the reaction diagram		Pseudomonas sp.--4751---
2-Oxopentanoate + L-Ala?
show the reaction diagram		Pseudomonas sp.--4751---
2-Oxopentanoate + L-Ala?
show the reaction diagram		Pseudomonas sp.-135% of the activity with 2-oxobutanoate4748---
alpha-Aminomalonate + pyruvateGly + ? + CO2
show the reaction diagram		Burkholderia cepacia-nonoxidative decarboxylation4754-4754-
alpha-Aminomalonate + pyruvate + O2Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754-4754-
Cycloleucine + pyruvateL-Ala + ? + CO2
show the reaction diagram		Fusarium solani--4757---
Cycloleucine + pyruvateL-Ala + ? + CO2
show the reaction diagram		Pseudomonas sp.-reverse of decarboxylation is not deteced, exchange transamination between L-Ala and pyruvate is reversible4751-4751-
D-Ala + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
D-Ala + pyruvateL-Ala + ? + CO2
show the reaction diagram		Fusarium solani-no activity4757---
Gly + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
Glyoxalate + DL-Ile?
show the reaction diagram		Pseudomonas sp.--4751---
Glyoxalate + L-Ala?
show the reaction diagram		Pseudomonas sp.--4751---
Isopropylamine + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
Isovaline + pyruvateL-Ala + butanone + CO2
show the reaction diagram		Burkholderia cepacia--664227--?
Isovaline + pyruvateL-Ala + butanone + CO2
show the reaction diagram		Pseudomonas sp.-,reverse of decarboxylation is not deteced, exchange transamination between L-Ala and pyruvate is reversible4751-4751-
L-Ala + 2-oxobutanoatePyruvate + ? + CO2
show the reaction diagram		Fusarium solani--4757---
L-Ala + 2-oxoisopentanoatePyruvate + ? + CO2
show the reaction diagram		Fusarium solani--4757---
L-Ala + 2-oxopentanoatePyruvate + ? + CO2
show the reaction diagram		Fusarium solani--4757---
L-Ala + glyoxylatePyruvate + ? + CO2
show the reaction diagram		Fusarium solani--4757---
L-Ala + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
L-Phenylglycine + pyruvateL-Ala + ? + CO2
show the reaction diagram		Burkholderia cepacia--4754---
Pyruvate + 2-aminoisobutanoate?
show the reaction diagram		Burkholderia cepacia--4756---
Pyruvate + DL-Ile?
show the reaction diagram		Pseudomonas sp.--4751---
Pyruvate + Gly?
show the reaction diagram		Burkholderia cepacia--4754---
Pyruvate + isopropylamine?
show the reaction diagram		Burkholderia cepacia--4754---
Pyruvate + L-Ala?
show the reaction diagram		Pseudomonas sp.--4751---
Pyruvate + L-Ala?
show the reaction diagram		Burkholderia cepacia--4754---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
No entries in this field

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateBurkholderia cepacia-enzyme contains bound pyridoxal phosphate4750 2D-image
pyridoxal 5'-phosphatePseudomonas sp.-required. Km: 0.005 mM4751 2D-image
pyridoxal 5'-phosphateBurkholderia cepacia-dependent on4752, 4753, 4756, 661129 2D-image
pyridoxal 5'-phosphateBurkholderia cepacia--4758 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ba2+Burkholderia cepacia-gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate661129
Ca2+Burkholderia cepacia-gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius661129
Cs+Burkholderia cepacia-activates to a lesser extent than K+661129
K+Burkholderia cepacia-activates4752, 664227
K+Burkholderia cepacia-activates; the K+-activated enzyme in solution exists in two conformations differing in catalytic competence4753
K+Burkholderia cepacia-activity is dependent on cations. K+ is the monovalent cation with the optimal size for catalytic activity, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate661129
Li+Burkholderia cepacia-activates to a lesser extent than K+661129
Na+Burkholderia cepacia-activates to a lesser extent than K+, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate661129
NH4+Burkholderia cepacia-activates to a lesser extent than K+661129
NH4+Burkholderia cepacia-activates664227
Rb+Burkholderia cepacia-activates4752, 4753
Rb+Burkholderia cepacia-activates to a lesser extent than K+661129
Tl+Burkholderia cepacia-activates to a lesser extent than K+661129
Mg2+Burkholderia cepacia-gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius661129
additional informationBurkholderia cepacia-a binding site for alkali metal ions is close to the active site. Exchange of K+ for Na+ at this site is shown to affect the conformation of two active site residues4752
additional informationBurkholderia cepacia-hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site4753

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(R)-1-amino-1-methylpropanephosphonateBurkholderia cepacia--650109 2D-image
(R)-1-amino-1-phenylethanephosphonateBurkholderia cepacia--650109 2D-image
(R)-1-aminoethanephosphonateBurkholderia cepacia--650109 2D-image
(S)-1-aminoethanephosphonateBurkholderia cepacia--650109 2D-image
1-amino-1-cyclopropane carboxylateBurkholderia cepacia-i.e. ACC652809 2D-image
1-aminocyclopentanephosphonateBurkholderia cepacia--650109 2D-image
1-aminocyclopropane 1-carboxylateBurkholderia cepacia--4753, 4755 2D-image
3,3,3-Trifluoro-2-aminoisobutanoateBurkholderia cepacia-irreversible, the inhibitor undergoes catalytic decarboxylation during the inactivation process and binds at the enzyme's active site4749 2D-image
5'-phosphopyridoxyl-2-methylalanineBurkholderia cepacia-i.e. PPL-MeAla652809 2D-image
D-cycloserineBurkholderia cepacia--4750 2D-image
D-cycloserineBurkholderia cepacia-competitive, L-isomer has 3000fold greater inhibitory potency than D-isomer652809 2D-image
GlyBurkholderia cepacia-competitive against 2-aminoisobutanoate4754 2D-image
HgCl2Fusarium solani--4757 2D-image
hydroxylamineFusarium solani--4757 2D-image
iodoacetamideFusarium solani--4757 2D-image
L-CycloserineBurkholderia cepacia--4750 2D-image
L-CycloserineFusarium solani--4757 2D-image
L-CycloserineBurkholderia cepacia-competitive, L-isomer has 3000fold greater inhibitory potency than D-isomer652809 2D-image
LactateBurkholderia cepacia--4755 2D-image
Na+Burkholderia cepacia--4752, 4753, 664227 2D-image
PCMBFusarium solani--4757 2D-image
phenylhydrazineFusarium solani--4757 2D-image
phosphono-2-methylalanineBurkholderia cepacia--652809 2D-image
pyruvateBurkholderia cepacia--4755 2D-image
Li+Burkholderia cepacia--4752, 4753 2D-image
additional informationBurkholderia cepacia-not inhibitory: pyruvate4756-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.12-2-aminoisobutanoateBurkholderia cepacia-enzyme with Na+ in the metal binding site4753 2D-image
2-2-aminoisobutanoateBurkholderia cepacia-enzyme with K+ in the metal binding site4753 2D-image
2-2-aminoisobutanoateBurkholderia cepacia-activated by K+661129 2D-image
2.2-2-aminoisobutanoateBurkholderia cepacia-activated by Rb+661129 2D-image
4.4-2-aminoisobutanoateBurkholderia cepacia-activated by NH4+661129 2D-image
5.8-2-aminoisobutanoateBurkholderia cepacia-activated by Mg2+661129 2D-image
6.6-2-aminoisobutanoateBurkholderia cepacia-activated by Tl+661129 2D-image
7.3-2-aminoisobutanoateBurkholderia cepacia-activated by Cs+661129 2D-image
8.7-2-aminoisobutanoateBurkholderia cepacia--4750 2D-image
8.7-2-aminoisobutanoateBurkholderia cepacia-enzyme with Na+ in the metal binding site4753 2D-image
11-2-aminoisobutanoateBurkholderia cepacia-activated by Li+661129 2D-image
13-2-aminoisobutanoateBurkholderia cepacia-activated by Na+661129 2D-image
18-2-aminoisobutanoateBurkholderia cepacia-activated by Ca2+661129 2D-image
30-2-aminoisobutanoateBurkholderia cepacia-pH 7.8, mutant enzyme Q52A661182 2D-image
66-2-aminoisobutanoateBurkholderia cepacia-activated by Ba2+661129 2D-image
2.2-2-aminoisobutyrateBurkholderia cepacia-pH 7.54756 2D-image
0.015-pyruvateBurkholderia cepacia-pH 7.8, mutant enzyme Q52A661182 2D-image
0.098-pyruvateBurkholderia cepacia-pH 7.54756 2D-image
0.17-pyruvateBurkholderia cepacia--4750 2D-image
2-pyruvatePseudomonas sp.--4751 2D-image
33-L-AlaPseudomonas sp.--4751 2D-image
additional information-additional informationBurkholderia cepacia--4755-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.3-1-amino-1-cyclohexanecarboxylateBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
0.98-1-amino-1-cyclopentanecarboxylateBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
0.05-2-aminoisobutanoateBurkholderia cepacia-activated by Ca2+661129 2D-image
0.076-2-aminoisobutanoateBurkholderia cepacia-activated by Mg2+661129 2D-image
0.12-2-aminoisobutanoateBurkholderia cepacia-pH 7.8, mutant enzyme Q52A661182 2D-image
0.86-2-aminoisobutanoateBurkholderia cepacia-activated by Li+661129 2D-image
1.29-2-aminoisobutanoateBurkholderia cepacia-enzyme with Na+ in the metal binding site4753 2D-image
1.4-2-aminoisobutanoateBurkholderia cepacia-activated by Ba2+661129 2D-image
1.83-2-aminoisobutanoateBurkholderia cepacia-activated by Na+661129 2D-image
3.8-2-aminoisobutanoateBurkholderia cepacia-activated by Cs+661129 2D-image
4.47-2-aminoisobutanoateBurkholderia cepacia-enzyme with Rb+ in the metal binding site4753 2D-image
4.9-2-aminoisobutanoateBurkholderia cepacia-activated by NH4+661129 2D-image
5.22-2-aminoisobutanoateBurkholderia cepacia-activated by Tl+661129 2D-image
7.4-2-aminoisobutanoateBurkholderia cepacia-activated by Rb+661129 2D-image
10.4-2-aminoisobutanoateBurkholderia cepacia-activated by K+661129 2D-image
13.1-2-aminoisobutanoateBurkholderia cepacia-enzyme with K+ in the metal binding site4753 2D-image
25-2-aminoisobutanoateBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
0.025-alpha-AminomalonateBurkholderia cepacia-with pyruvate as cosubstrate, oxidative decarboxylation4754 2D-image
0.2-D-AlaBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
0.0012-GlyBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
0.12-pyruvateBurkholderia cepacia-pH 7.8, mutant enzyme Q52A661182 2D-image
0.033-L-AlaBurkholderia cepacia-with pyruvate as cosubstrate, decarboxylation4754 2D-image
additional information-additional informationBurkholderia cepacia--4755-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4.9-(R)-1-amino-1-methylpropanephosphonateBurkholderia cepacia-pH 7.8, homologous to L-isovaline650109 2D-image
13-(R)-1-amino-1-phenylethanephosphonateBurkholderia cepacia-pH 7.8, homologous to L-phenylglycine650109 2D-image
19-(R)-1-aminoethanephosphonateBurkholderia cepacia-pH 7.8, homologous to L-alanine650109 2D-image
1.1-(S)-1-aminoethanephosphonateBurkholderia cepacia-pH 7.8, homologous to D-alanine650109 2D-image
6-1-aminocyclopentanephosphonateBurkholderia cepacia-pH 7.8, homologous to aminocyclopropane carboxylate650109 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2.43-Burkholderia cepacia--4759
3.2-Fusarium solani--4757
8.8-Burkholderia cepacia--4750
additional information-Pseudomonas sp.--4751

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
8-Fusarium solani--4757
8.5-Burkholderia cepacia--664227

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
610Fusarium solani-pH 6.0: about 30% of maximal activity, pH 10.0: about 70% of maximal activity4757
additional information-Burkholderia cepacia-pH-dependence of transamination half-reaction4756

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
60-Fusarium solani--4757

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
myceliumFusarium solani--4757Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
1d7r, downloadSCOP (1d7r)CATH (1d7r)Burkholderia cepacia
1d7s, downloadSCOP (1d7s)CATH (1d7s)Burkholderia cepacia
1d7u, downloadSCOP (1d7u)CATH (1d7u)Burkholderia cepacia
1d7v, downloadSCOP (1d7v)CATH (1d7v)Burkholderia cepacia
1dgd, downloadSCOP (1dgd)CATH (1dgd)Burkholderia cepacia
1dge, downloadSCOP (1dge)CATH (1dge)Burkholderia cepacia
1dka, downloadSCOP (1dka)CATH (1dka)Burkholderia cepacia
1m0n, downloadSCOP (1m0n)CATH (1m0n)Burkholderia cepacia
1m0o, downloadSCOP (1m0o)CATH (1m0o)Burkholderia cepacia
1m0p, downloadSCOP (1m0p)CATH (1m0p)Burkholderia cepacia
1m0q, downloadSCOP (1m0q)CATH (1m0q)Burkholderia cepacia
1z3z, downloadSCOP (1z3z)CATH (1z3z)Burkholderia cepacia
1zc9, downloadSCOP (1zc9)CATH (1zc9)Burkholderia cepacia
1zob, downloadSCOP (1zob)CATH (1zob)Burkholderia cepacia
1zod, downloadSCOP (1zod)CATH (1zod)Burkholderia cepacia
2dkb, downloadSCOP (2dkb)CATH (2dkb)Burkholderia cepacia

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
166000-Fusarium solani-gel filtration4757
188000-Burkholderia cepacia-equilibrium sedimentation4750

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
tetramerBurkholderia cepacia-4 * 47000, ultracentrifugal analysis in presence of 8 M urea or 7 M guanidine HCl4750
tetramerFusarium solani-4 * 42000, SDS-PAGE4757
tetramerBurkholderia cepacia-4 * 46500, alpha4, calculation from crystallographic data4758
tetramerBurkholderia cepacia-4 * 46500, SDS-PAGE664227

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Burkholderia cepacia-4750, 4758
crystal structure at 2.8 A resolution of tzhe enzyme with Li+ or Rb+ bound; crystal structures at 2.8 A resolution with Li+ and Rb+ bound at the binding site for alkali metal ions which is close to the active site, i.e. site 1Burkholderia cepacia-4752
hanging drop vapor diffusion method, crystal structure of Q52A mutant and wild-type enzyme in complex with pyridoxamine 5'-phosphateBurkholderia cepacia-661182
in complex with different aminophosphonate inhibitorsBurkholderia cepacia-650109
in complex with four inhibitorsBurkholderia cepacia-652809

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
60-Fusarium solani-30 min, completely stable4757
70-Fusarium solani-30 min, 85% loss of activity4757

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Burkholderia cepacia-4750, 661182
recombinant enzymeBurkholderia cepacia-4759
-Fusarium solani-4757
-Pseudomonas sp.-4751

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliBurkholderia cepacia-4753, 4759
-Mycosphaerella graminicolaQ7Z8J1650912

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Q52ABurkholderia cepacia-85fold decrease in turnover number for decarboxylation half-reaction with 2-aminoisobutyrate and pyruvate, greatly reduced rate of transamination half-reaction and impaired pyridoxamine phosphate binding661182
Q52EBurkholderia cepacia-10000fold decrease in turnover number for decarboxylation half-reaction with 2-aminoisobutyrate and pyruvate, transamination rate is nearly identical to wild-type value661182
Q52IBurkholderia cepacia-100000fold decrease in turnover number for decarboxylation half-reaction with 2-aminoisobutyrate and pyruvate, greatly reduced rate of transamination half-reaction and impaired pyridoxamine phosphate binding661182
additional informationMycosphaerella graminicolaQ7Z8J1gene knockout mutants display wild-type morphology and pathogenicity, can use alanine as sole nitrogen source, but not 2-methylalanine650912

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
4748Koide, Y.; Honma, M.; Shimomura, T.L-Alanine-alpha-ketobutyrate aminotransferase of Pseudomonas sp.Agric. Biol. Chem.45775-7761981Pseudomonas sp.-
4749Keller, J.W.; O'Leary, M.H.3,3,3-Trifluoro-2-aminoisobutyrate: a mechanism-based inhibitor of Pseudomonas cepacia alpha-dialkylamino acidBiochem. Biophys. Res. Commun.901104-11101979Burkholderia cepacia PubMed
4750Lamatiniere, C.A.; Itho, H.; Dempsey, W.B.alpha-Dialkyl acid transaminase from Pseudomonas cepacia. Purification, crystallization, physical, and kinetic propertiesBiochemistry104783-47881971Burkholderia cepacia PubMed
4751Bailey, G.B.; Dempsey, W.B.Purification and properties of an alpha-dialkyl amino acid transaminaseBiochemistry61526-15331967Pseudomonas sp.-
4752Hohenester, E.; Keller, J.W.; Jansonius, J.N.An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylaseBiochemistry3313561-135701994Burkholderia cepacia PubMed
4753Zhou, X.; Kay, S.; Toney, M.D.Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ionsBiochemistry375761-57691998Burkholderia cepacia PubMed
4754Sun, S.; Zabinski, R.F.; Toney, M.D.Reactions of alternate substrates demonstrate stereoelectronic control of reactivity in dialkylglycine decarboxylaseBiochemistry373865-38751998Burkholderia cepacia PubMed
4755Sun, S.; Bagdassarian, C.K.; Toney, M.D.Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylaseBiochemistry373876-38851998Burkholderia cepacia PubMed
4756Zhou, X.; Toney, M.D.pH Studies on the mechanism of the pyridoxal phosphate-dependent dialkylglycine decarboxylaseBiochemistry38311-3201999Burkholderia cepacia PubMed
4757Esaki, N.; Watanabe, M.; Kurihara, T.; Soda, K.Fungal thermostable alpha-dialkylamino acid aminotransferase: occurence, purification and characterizationArch. Microbiol.161110-1151994Aspergillus candidus, Aspergillus oryzae, Aspergillus parasiticus, Aspergillus sojae, Fusarium merismoides, Fusarium solani, Mucor globosus-
4758Toney, M.D.; Hohenester, E.; Keller, J.W.; Jansonius, J.N.Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylaseJ. Mol. Biol.245151-1791995Burkholderia cepacia PubMed
4759Keller, J.W.; Baurick, K.B.; Rutt., G.C.; O'Malley, M.V.; Sonafrank, N.L.; Reynolds, R.A.; Ebbesson, L.O.E.; Vajdos, F.F.Pseudomonas cepacia 2,2-dialkylglycine decarboxylaseJ. Biol. Chem.2655531-55391990Burkholderia cepacia PubMed
650033Zhou, X.; Jin, X.; Medhekar, R.; Chen, X.; Dieckmann, T.; Toney, M.D.Rapid kinetic and isotopic studies on dialkylglycine decarboxylaseBiochemistry401367-13772001Burkholderia cepacia PubMed
650109Liu, W.; Rogers, C.J.; Fisher, A.J.; Toney, M.D.Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibitionBiochemistry4112320-123282002Burkholderia cepacia PubMed
650912Adachi, K.; Nelson, G.H.; Peoples, K.A.; DeZwaan, T.M.; Skalchunes, A.R.; Heiniger, R.W.; Shuster, J.R.; Hamer, L.; Tanzer, M.M.Sequence analysis and functional characterization of the dialkylglycine decarboxylase gene DGD1 from Mycosphaerella graminicolaCurr. Genet.43358-3632003Mycosphaerella graminicola PubMed
652809Malashkevich, V.N.; Strop, P.; Keller, J.W.; Jansonius, J.N.; Toney, M.D.Crystal structures of dialkylglycine decarboxylase inhibitor complexesJ. Mol. Biol.294193-2001999Burkholderia cepacia PubMed
661129Liu, W.; Toney, M.D.Kinetic and thermodynamic analysis of the interaction of cations with dialkylglycine decarboxylaseBiochemistry434998-50102004Burkholderia cepacia PubMed
661182Fogle, E.J.; Liu, W.; Woon, S.T.; Keller, J.W.; Toney, M.D.Role of Q52 in catalysis of decarboxylation and transamination in dialkylglycine decarboxylaseBiochemistry4416392-164042005Burkholderia cepacia PubMed
664227Schnackerz, K.D.; Keller, J.; Phillips, R.S.; Toney, M.D.Ionization state of pyridoxal 5'-phosphate in d-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by (31)P NMR spectroscopyBiochim. Biophys. Acta1764230-2382006Burkholderia cepacia PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.64)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)