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Information on EC 4.1.1.1 - pyruvate decarboxylase and Organism(s) Zymomonas mobilis and UniProt Accession P06672
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4.1.1.1 pyruvate decarboxylaseIUBMB Comments
A thiamine-diphosphate protein. Also catalyses acyloin formation.
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Word Map
- 4.1.1.1
- dendritic
-
plasmacytoid
-
toll-like
- thiamin
-
claim
- autoimmune
-
prescript
- ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
- zymomonas
-
branched-chain
- cdc
- acetaldehyde
- mobilis
- sulfonylurea
-
real-world
-
tregs
-
adhes
- interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
- statin
-
costimulatory
-
lipoylated
- erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
- dabigatran
- acetolactate
-
marketscan
-
dispensing
- synthesis
-
hla-dr
-
antimitochondrial
- acetoin
-
dihydrolipoyl
- biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
- dihydrolipoamide
- transacetylase
- rivaroxaban
- dichloroacetate
-
enrollees
- lipoate
The taxonomic range for the selected organisms is: Zymomonas mobilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pdc, pyruvate decarboxylase, acetohydroxyacid synthase, yeast pyruvate decarboxylase, pdc1p, ifpl730, p59nc, zmpdc, pyruvate decarboxylase 1, pdc5p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8-10 nm cytoplasmic filament-associated protein
-
-
-
-
alpha-Carboxylase
-
-
-
-
alpha-Keto acid carboxylase
-
-
-
-
Decarboxylase, pyruvate
-
-
-
-
P59NC
-
-
-
-
PDC
Pyruvic decarboxylase
-
-
-
-
PDC
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 2-oxo carboxylate = an aldehyde + CO2
in absence of substrate, equilibrium is shifted to 4'-aminopyridine thiamine diphosphate. Carbonyl group of substrate forms a hydrogen bond to Tyr290, geometry of substrate is well-suited for a nucleophilic attack by ylide-thiamine diphosphate
a 2-oxo carboxylate = an aldehyde + CO2
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions, thermodynamic data
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-oxo-acid carboxy-lyase (aldehyde-forming)
A thiamine-diphosphate protein. Also catalyses acyloin formation.
CAS REGISTRY NUMBER
COMMENTARY
9001-04-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoylformate
benzaldehyde + CO2
substrate only for mutant mutant I472A
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae
(R)-phenylacetylcarbinol
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
wild-type 100% conversion, 98% enantiomeric excess, mutant I472A, 60% conversion, 70% enantiomeric excess, mutant I476E, 6% conversion, 60% enantiomeric excess of S-enantiomer
-
-
?
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate
acetaldehyde + CO2
C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
active site structure, catalytic mechanism
-
?
pyruvate
acetaldehyde + CO2
-
H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
catalyzes the penultimate step in ethanol fermentation
-
?
additional information
?
-
PDC has no activity with benzoylformate
-
-
?
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate
acetaldehyde + CO2
-
catalyzes the penultimate step in ethanol fermentation
-
?
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
Mg2+
-
cofactor, mode of active site binding, contains 1 mol Mg2+ per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphoryldifluoromethyl)phosphonic acid
-
-
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphorylmethyl) phosphonic acid
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethanol
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-5-methyl-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a thiamine diphosphate analogue, almost irreversible inhibition
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a methyl triazole analogue of thiamine diphosphate, almost irreversible inhibition
3-deazathiamine diphosphate
-
12-step synthesis of the isoelectronic thiophene analogue of thiamine diphosphate, overview
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
N-([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]sulfonyl)phosphoramidic acid
-
-
O-2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl sulfamate
-
-
[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)sulfonyl]phosphoramidic acid
-
a phosphoramidic acid thiamine diphosphate analogue
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl](difluoro)methyl]phosphonic acid
-
a difluoromethylenediphosphonate ester thiamine diphosphate analogue
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl]methyl]phosphonic acid
-
a methylenediphosphonate ester thiamine diphosphate analogue
additional information
-
no product inhibition by (R)-1-phenyl-1-hydroxy-propane-2-one
-
benzaldehyde
-
after a 20 h incubation with 30 mM benzaldehyde, the residual activity is 84% of the initial activity, enzyme stability dramatically decreases in the presence of 200 mM benzaldehyde (27% residual activity after 3 h incubation)
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
high glycolytic and ethanologenic fluxes correlate with enhanced transcription and enzymatic activity levels of PDC
-
additional information
-
PDC activity in KO11 is limiting and hence positively controls the flux to ethanol formation, since a 7fold amplification of its activity causes a 1.3fold increase into the ethanol flux, increased PDC activity stimulates glucose and xylose consumption rates
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.31
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.4
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
additional information
additional information
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
kinetic data, kinetic model
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.15
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
150
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
additional information
additional information
values for several C-terminal deletion mutants
-
additional information
additional information
-
values for several C-terminal deletion mutants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.67
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
484
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000095
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphoryldifluoromethyl)phosphonic acid
-
-
0.0000012
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphorylmethyl) phosphonic acid
-
-
0.3
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethanol
-
-
0.00000003
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
0.00000002
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-5-methyl-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
0.00000003
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
-
0.00000002
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
-
0.4
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
0.4
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
0.00014
N-([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]sulfonyl)phosphoramidic acid
-
-
0.008
O-2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl sulfamate
-
-
0.00014
[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)sulfonyl]phosphoramidic acid
-
-
0.00000095
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl](difluoro)methyl]phosphonic acid
-
-
0.0000012
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl]methyl]phosphonic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
-
carboligation of acetaldehyde and benzaldehyde, optimal activity in potassium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 8
-
pH 4.6: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
-
only slightly differing catalytic activity in the range, +/-10% relative to 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
240000
60000
60000
-
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
phosphate stabilizes the tetramer by shifting the dimer-tetramer equilibrium to higher pH values, without altering the conformation of the tetramer
tetramer
-
two of the dimers form a tightly packed tetramer with pseudo 222 symmetry
tetramer
-
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using potassium fluoride (0.2 M) and PEG 3350 (20% w/v), cocrystallization of PDC with pyruvate is conducted using a reservoir solution containing potassium chloride (0.2 M), PEG 3350 (17% w/v), and xylitol (3 or 1.5%, (w/v))
hanging drop vapor diffusion method, using 100 mM MES buffer (pH 6.0), 1 mM thiamin diphosphate, 5 mM MgSO4, and 20-24% (w/v) polyethylene glycol 1500
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I472A/I476F
increase in substrate binding affinity and specificity, highest enantioselectivity for (S)-acetoin, very low yield of product
I476F
rapid loss of cofactor thiamine diphosphate. Improvement of enantioselectivity for (S)-acetoin
mutant I472A
2fold decrease in pyruvate decarboxylase activity, switch in substrate specificity to catalyse decarboxylation of benzoylformate, chimera between pyruvate decarboxylase and benzoylformate decarboxylase. Preferred substrates are 2-ketopentanoic acid and 2-ketohexanoic acid. Improvement of enantioselectivity for (S)-acetoin
D27E
-
0.072% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D27N
-
0.049% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D440E
-
active, but unlike the wild type enzyme, exhibits a lag phase in product formation which can be reduced by preincubation with 5 mM thiamine diphosphate. Mutant N467D shows decreased affinity for thiamine diphosphate
E473D
E473Q
I472A
-
mutation influences the decarboxylation and carboligation reactions. The enlarged substrate-binding site allows the decarboxylation of longer aliphatic 2-keto acids (C4-C6) as well as aromatic 2-keto acids besides pyruvate, yielding hydroxypropiophenone, benzoin and phenylacetylcarbinol. Mutation impairs enantioselectivity
I476A
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476E
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476L
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476V
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
N482D
-
mutation has a significant influence on the carboligation reaction, the binding of the cofactors and the thermostability are not affected
W329M
-
the carboligase activity of the mutant is 2.8% as high as the decarboxylase activity which is about 10fold higher than the wild type enzyme
W392M
-
higher carboligase/(R)-phenylacetylcarbinol-producing activity, more stable and higher resistance towards acetaldehyde than wild-type PDC
additional information
E473D
-
0.173% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
E473D
-
the mutant exhibits a residual activity of 0.6% compared to the wild type enzyme, wild type PDC and the Glu473Asp variant bind the substrate analogue acetylphosphinate with the same affinity
E473Q
-
0.025% of wild-type specific activity, more tightly bound cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
E473Q
-
the mutant exhibits a residual activity of 0.1% compared to the wild type enzyme, Glu473Gln fails to bind the substrate analogue acetylphosphinate
additional information
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
-
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
-
enhancement of 1,3-propanediol production by expression of functional pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae. The acetolactate synthase-deficient mutant of Klebsiella pneumoniae fails to produce 1,3-propanediol or 2,3-butanediol, and is defective in glycerol metabolism
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more stable than PDC from Saccharomyces cerevisiae, stirring deactivates significantly
-
retains about 50% of activity in buffer supplemented with 2 M NaCl or KCl, retain 20% of activity in 4 M salt buffer
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type PDC and C-terminal deletion mutants in Escherichia coli
expression of PDC mutants D27E, D27N, E473D and E473Q in Escherichia coli
-
fused with alcohol dehydrogenase and expressed in Escherichia coli JM109 cells
-
gene pdc, recombinant expression in an acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
-
wild type enzyme is expressed in Escherichia coli SG13009 cells, mutant enzymes E473D and E473Q are expressed in Escherichia coli JM109 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
synthesis of (R)-phenylacetylcarbinol from cheap substrates in an aqueous reaction system by W392M mutant PDC, alternative strategy to the current fermentative process free of any unwanted by-product
synthesis
enhancement of ethanol production capacity of Clostridium thermocellum by transferring pyruvate decarboxylase and alcohol dehydrogenase genes of the homoethanol pathway from Zymomonas mobilis. Both transferring pyruvate decarboxylase and alcohol dehydrogenase are functional in Clostridium thermocellum, but the presence of and alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Neale, A.D.; Scopes, R.K.; Wettenhall, R.E.H.; Hoogenraad, N.J.
Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli
J. Bacteriol.
169
1024-1028
1987
Zymomonas mobilis
Bringer-Meyer, S.; Schimz, K.L.; Sahm, H.
Pyruvate decarboxylase from Zymomonas mobilis. Isolation and partial characterization
Arch. Microbiol.
146
105-110
1986
Zymomonas mobilis
-
Hoppner, T.C.; Doelle, H.W.
Purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production
Eur. J. Appl. Microbiol. Biotechnol.
17
152-157
1983
Zymomonas mobilis
-
Candy, J.M.; Duggleby, R.G.
Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme
Biochim. Biophys. Acta
1385
323-338
1998
Acetobacter sp., Aspergillus sp., Saccharomyces cerevisiae, Canavalia ensiformis, Citrus sp., Clostridium botulinum, Erwinia amylovora, Hanseniaspora uvarum, Ipomoea batatas, Kluyveromyces sp., Neurospora crassa, Pastinaca sativa, Pisum sativum, Saccharomyces pastorianus, Saccharomyces uvarum, Sarcina ventriculi, Schizosaccharomyces pombe, Zea mays, Zymomonas mobilis
Dobritzsch, D.; Knig, S.; Schneider, G.; Lu, G.
High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases
J. Biol. Chem.
273
20196-20204
1998
Zymomonas mobilis
Miczka, G.; Vernau, J.; Kula, M.R.; Hoffmann, B.; Schomburg, D.
Purification and primary structure of pyruvate decarboxylase from Zymomonas mobilis
Biotechnol. Appl. Biochem.
15
192-206
1992
Zymomonas mobilis
Chang, A.K.; Nixon, P.F.; Duggleby, R.G.
Aspartate-27 and glutamate-473 are involved in catalysis by Zymomonas mobilis pyruvate decarboxylase
Biochem. J.
339
255-260
1999
Zymomonas mobilis
-
Chang, A.K.; Nixon, P.F.; Duggleby, R.G.
Effects of deletions at the carboxyl terminus of Zymomonas mobilis pyruvate decarboxylase on the kinetic properties and substrate specificity
Biochemistry
39
9430-9437
2000
Zymomonas mobilis (P06672), Zymomonas mobilis
Wang, J.; Golbik, R.; Seliger, B.; Spinka, M.; Tittmann, K.; Hubner, G.; Jordan, F.
Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase
Biochemistry
40
1755-1763
2001
Saccharomyces cerevisiae, Zymomonas mobilis
Goetz, G.; Iwan, P.; Hauer, B.; Breuer, M.; Pohl, M.
Continuous production of (R)-phenylacetylcarbinol in an enzyme-membrane reactor using a potent mutant of pyruvate decarboxylase from Zymomonas mobilis
Biotechnol. Bioeng.
74
317-325
2001
Saccharomyces cerevisiae, Zymomonas mobilis
Kaczowka, S.J.; Reuter, C.J.; Talarico, L.A.; Maupin-Furlow, J.A.
Recombinant production of Zymomonas mobilis pyruvate decarboxylase in the haloarchaeon Haloferax volcanii
Archaea
1
327-334
2005
Zymomonas mobilis
Lie, M.A.; Celik, L.; Jorgensen, K.A.; Schiott, B.
Cofactor activation and substrate binding in pyruvate decarboxylase. Insights into the reaction mechanism from molecular dynamics simulations
Biochemistry
44
14792-14806
2005
Zymomonas mobilis (P06672), Zymomonas mobilis
Siegert, P.; McLeish, M.J.; Baumann, M.; Iding, H.; Kneen, M.M.; Kenyon, G.L.; Pohl, M.
Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida
Protein Eng. Des. Sel.
18
345-357
2005
Zymomonas mobilis (P06672), Zymomonas mobilis
Erixon, K.M.; Dabalos, C.L.; Leeper, F.J.
Inhibition of pyruvate decarboxylase from Z. mobilis by novel analogues of thiamine pyrophosphate: investigating pyrophosphate mimics
Chem. Commun. (Camb. )
2007
960-962
2007
Zymomonas mobilis
Orencio-Trejo, M.; Flores, N.; Escalante, A.; Hernandez-Chavez, G.; Bolivar, F.; Gosset, G.; Martinez, A.
Metabolic regulation analysis of an ethanologenic Escherichia coli strain based on RT-PCR and enzymatic activities
Biotechnol. Biofuels
1(1)
8
2008
Zymomonas mobilis
Yun, H.; Kim, B.
Enzymatic production of (R)-phenylacetylcarbinol by pyruvate decarboxylase from Zymomonas mobilis
Biotechnol. Bioprocess Eng.
13
372-376
2008
Zymomonas mobilis
-
Thompson, A.H.; Studholme, D.J.; Green, E.M.; Leak, D.J.
Heterologous expression of pyruvate decarboxylase in Geobacillus thermoglucosidasius
Biotechnol. Lett.
30
1359-1365
2008
Zymomonas mobilis
Wang, Z.; Chen, M.; Xu, Y.; Li, S.; Lu, W.; Ping, S.; Zhang, W.; Lin, M.
An ethanol-tolerant recombinant Escherichia coli expressing Zymomonas mobilis pdc and adhB genes for enhanced ethanol production from xylose
Biotechnol. Lett.
30
657-663
2008
Zymomonas mobilis
Huerta-Beristain, G.; Utrilla, J.; Hernandez-Chavez, G.; Bolivar, F.; Gosset, G.; Martinez, A.
Specific ethanol production rate in ethanologenic Escherichia coli strain KO11 is limited by pyruvate decarboxylase
J. Mol. Microbiol. Biotechnol.
15
55-64
2008
Zymomonas mobilis
Erixon, K.M.; Dabalos, C.L.; Leeper, F.J.
Synthesis and biological evaluation of pyrophosphate mimics of thiamine pyrophosphate based on a triazole scaffold
Org. Biomol. Chem.
6
3561-3572
2008
Zymomonas mobilis
Yep, A.; McLeish, M.J.
Engineering the substrate binding site of benzoylformate decarboxylase
Biochemistry
48
8387-8395
2009
Zymomonas mobilis (P06672), Zymomonas mobilis
Pei, X.Y.; Erixon, K.M.; Luisi, B.F.; Leeper, F.J.
Structural insights into the prereaction state of pyruvate decarboxylase from Zymomonas mobilis
Biochemistry
49
1727-1736
2010
Zymomonas mobilis (P06672), Zymomonas mobilis
Hong, W.K.; Kim, C.H.; Heo, S.Y.; Luo, L.H.; Oh, B.R.; Seo, J.W.
Enhanced production of ethanol from glycerol by engineered Hansenula polymorpha expressing pyruvate decarboxylase and aldehyde dehydrogenase genes from Zymomonas mobilis
Biotechnol. Lett.
32
1077-1082
2010
Zymomonas mobilis
Meyer, D.; Neumann, P.; Parthier, C.; Friedemann, R.; Nemeria, N.; Jordan, F.; Tittmann, K.
Double duty for a conserved glutamate in pyruvate decarboxylase: evidence of the participation in stereoelectronically controlled decarboxylation and in protonation of the nascent carbanion/enamine intermediate
Biochemistry
49
8197-8212
2010
Zymomonas mobilis
Lee, S.M.; Hong, W.K.; Heo, S.Y.; Park, J.M.; Jung, Y.R.; Oh, B.R.; Joe, M.H.; Seo, J.W.; Kim, C.H.
Enhancement of 1,3-propanediol production by expression of pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
J. Ind. Microbiol. Biotechnol.
41
1259-1266
2014
Zymomonas mobilis, Zymomonas mobilis ZM4
Kannuchamy, S.; Mukund, N.; Saleena, L.M.
Genetic engineering of Clostridium thermocellum DSM1313 for enhanced ethanol production
BMC Biotechnol.
16
34
2016
Zymomonas mobilis (D9J047), Zymomonas mobilis
Pohl, M.; Siegert, P.; Mesch, K.; Bruhn, H.; Groetzinger, J.
Active site mutants of pyruvate decarboxylase from Zymomonas mobilis: A site-directed mutagenesis study of L112, I472, I476, E473, and N482
Eur. J. Biochem.
257
538-546
1998
Zymomonas mobilis
Lewicka, A.J.; Lyczakowski, J.J.; Blackhurst, G.; Pashkuleva, C.; Rothschild-Mancinelli, K.; Tautvaisas, D.; Thornton, H.; Villanueva, H.; Xiao, W.; Slikas, J.; Horsfall, L.; Elfick, A.; French, C.
Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in Escherichia coli
ACS Synth. Biol.
3
976-978
2014
Zymomonas mobilis
Yang, M.; Li, X.; Bu, C.; Wang, H.; Shi, G.; Yang, X.; Hu, Y.; Wang, X.
Pyruvate decarboxylase and alcohol dehydrogenase overexpression in Escherichia coli resulted in high ethanol production and rewired metabolic enzyme networks
World J. Microbiol. Biotechnol.
30
2871-2883
2014
Zymomonas mobilis
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