Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
mechanism
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
kinetics of inhibition
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
mechanism
-
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
cooperativity does not play a role in catalysis or regulation
-
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
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 Calpha
-
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
pH-studies on the mechanism
-
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
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 step
-
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine
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-reaction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,2-dialkylglycine + pyruvate
dialkyl ketone + CO2 + L-alanine
-
-
-
?
2-Aminoisobutanoate + pyruvate
L-Ala + acetone + CO2
-
-
-
?
1-Amino-1-cyclohexane-carboxylate + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
1-Amino-1-cyclopentane-carboxylate + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
2-Aminoisobutanoate + pyruvate
L-Ala + acetone + CO2
2-aminoisobutyrate + pyruvate
L-Ala + acetone + CO2
alpha-Aminomalonate + pyruvate
Gly + ? + CO2
-
nonoxidative decarboxylation
-
?
alpha-Aminomalonate + pyruvate + O2
Ala + ? + CO2
-
-
-
?
D-Ala + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
Gly + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
Isopropylamine + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
Isovaline + pyruvate
L-Ala + butanone + CO2
-
-
-
-
?
L-Ala + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
L-Phenylglycine + pyruvate
L-Ala + ? + CO2
-
-
-
-
?
Pyruvate + 2-aminoisobutanoate
?
-
-
-
-
?
Pyruvate + Gly
?
-
-
-
-
?
Pyruvate + isopropylamine
?
-
-
-
-
?
Pyruvate + L-Ala
?
-
-
-
-
?
2-Aminoisobutanoate + pyruvate
L-Ala + acetone + CO2
-
-
-
-
?
2-Aminoisobutanoate + pyruvate
L-Ala + acetone + CO2
-
-
-
?
2-Aminoisobutanoate + pyruvate
L-Ala + acetone + CO2
-
-
-
-
?
2-aminoisobutyrate + pyruvate
L-Ala + acetone + CO2
-
-
-
?
2-aminoisobutyrate + pyruvate
L-Ala + acetone + CO2
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ba2+
-
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'-phosphate
Ca2+
-
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius
Cs+
-
activates to a lesser extent than K+
Li+
-
activates to a lesser extent than K+
Mg2+
-
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius
Na+
-
activates to a lesser extent than K+, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate
Tl+
-
activates to a lesser extent than K+
K+
-
activates
K+
-
the K+-activated enzyme in solution exists in two conformations differing in catalytic competence
K+
-
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'-phosphate
NH4+
-
activates
NH4+
-
activates to a lesser extent than K+
Rb+
-
activates
Rb+
-
activates to a lesser extent than K+
additional information
-
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 residues
additional information
-
hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12
2-aminoisobutanoate
pH 7.8, mutant enzyme Q52A
0.12
pyruvate
pH 7.8, mutant enzyme Q52A
2.3
1-amino-1-cyclohexanecarboxylate
-
with pyruvate as cosubstrate, decarboxylation
0.98
1-amino-1-cyclopentanecarboxylate
-
with pyruvate as cosubstrate, decarboxylation
0.05 - 25
2-aminoisobutanoate
0.025
alpha-aminomalonate
-
with pyruvate as cosubstrate, oxidative decarboxylation
0.2
D-Ala
-
with pyruvate as cosubstrate, decarboxylation
0.0012
Gly
-
with pyruvate as cosubstrate, decarboxylation
0.033
L-Ala
-
with pyruvate as cosubstrate, decarboxylation
additional information
additional information
-
-
-
0.05
2-aminoisobutanoate
-
activated by Ca2+
0.076
2-aminoisobutanoate
-
activated by Mg2+
0.86
2-aminoisobutanoate
-
activated by Li+
1.29
2-aminoisobutanoate
-
enzyme with Na+ in the metal binding site
1.4
2-aminoisobutanoate
-
activated by Ba2+
1.83
2-aminoisobutanoate
-
activated by Na+
3.8
2-aminoisobutanoate
-
activated by Cs+
4.47
2-aminoisobutanoate
-
enzyme with Rb+ in the metal binding site
4.9
2-aminoisobutanoate
-
activated by NH4+
5.22
2-aminoisobutanoate
-
activated by Tl+
7.4
2-aminoisobutanoate
-
activated by Rb+
10.4
2-aminoisobutanoate
-
activated by K+
13.1
2-aminoisobutanoate
-
enzyme with K+ in the metal binding site
25
2-aminoisobutanoate
-
with pyruvate as cosubstrate, decarboxylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Keller, J.W.; O'Leary, M.H.
3,3,3-Trifluoro-2-aminoisobutyrate: a mechanism-based inhibitor of Pseudomonas cepacia alpha-dialkylamino acid
Biochem. Biophys. Res. Commun.
90
1104-1110
1979
Burkholderia cepacia
brenda
Lamatiniere, C.A.; Itho, H.; Dempsey, W.B.
alpha-Dialkyl acid transaminase from Pseudomonas cepacia. Purification, crystallization, physical, and kinetic properties
Biochemistry
10
4783-4788
1971
Burkholderia cepacia
brenda
Hohenester, E.; Keller, J.W.; Jansonius, J.N.
An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase
Biochemistry
33
13561-13570
1994
Burkholderia cepacia
brenda
Zhou, X.; Kay, S.; Toney, M.D.
Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions
Biochemistry
37
5761-5769
1998
Burkholderia cepacia
brenda
Sun, S.; Zabinski, R.F.; Toney, M.D.
Reactions of alternate substrates demonstrate stereoelectronic control of reactivity in dialkylglycine decarboxylase
Biochemistry
37
3865-3875
1998
Burkholderia cepacia
brenda
Sun, S.; Bagdassarian, C.K.; Toney, M.D.
Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylase
Biochemistry
37
3876-3885
1998
Burkholderia cepacia
brenda
Zhou, X.; Toney, M.D.
pH Studies on the mechanism of the pyridoxal phosphate-dependent dialkylglycine decarboxylase
Biochemistry
38
311-320
1999
Burkholderia cepacia
brenda
Toney, 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 decarboxylase
J. Mol. Biol.
245
151-179
1995
Burkholderia cepacia (P16932)
brenda
Keller, 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 decarboxylase
J. Biol. Chem.
265
5531-5539
1990
Burkholderia cepacia
brenda
Zhou, X.; Jin, X.; Medhekar, R.; Chen, X.; Dieckmann, T.; Toney, M.D.
Rapid kinetic and isotopic studies on dialkylglycine decarboxylase
Biochemistry
40
1367-1377
2001
Burkholderia cepacia
brenda
Liu, W.; Rogers, C.J.; Fisher, A.J.; Toney, M.D.
Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition
Biochemistry
41
12320-12328
2002
Burkholderia cepacia (P16932)
brenda
Malashkevich, V.N.; Strop, P.; Keller, J.W.; Jansonius, J.N.; Toney, M.D.
Crystal structures of dialkylglycine decarboxylase inhibitor complexes
J. Mol. Biol.
294
193-200
1999
Burkholderia cepacia (P16932)
brenda
Liu, W.; Toney, M.D.
Kinetic and thermodynamic analysis of the interaction of cations with dialkylglycine decarboxylase
Biochemistry
43
4998-5010
2004
Burkholderia cepacia
brenda
Fogle, E.J.; Liu, W.; Woon, S.T.; Keller, J.W.; Toney, M.D.
Role of Q52 in catalysis of decarboxylation and transamination in dialkylglycine decarboxylase
Biochemistry
44
16392-16404
2005
Burkholderia cepacia (P16932)
brenda
Schnackerz, 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 spectroscopy
Biochim. Biophys. Acta
1764
230-238
2006
Burkholderia cepacia
brenda
Bassyouni, F.A.; Saleh, T.S.; ElHefnawi, M.M.; Abd El-Moez, S.I.; El-Senousy, W.M.; Abdel-Rehim, M.E.
Synthesis, pharmacological activity evaluation and molecular modeling of new polynuclear heterocyclic compounds containing benzimidazole derivatives
Arch. Pharm. Res.
35
2063-2075
2012
Burkholderia cepacia (P16932)
brenda