3.6.1.1: inorganic diphosphatase
This is an abbreviated version!
For detailed information about inorganic diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.1
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3.6.1.1
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thiamine
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ppases
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vacuole
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apparatus
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nucleoside
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tonoplast
-
triphosphate
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cytochemical
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cisternae
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h+-atpase
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lysosome
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magnesium
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polyphosphate
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glucose-6-phosphatase
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orthophosphate
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mung
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rubrum
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cytochemistry
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rhodospirillum
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imidodiphosphate
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saccule
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nudix
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h+-pumping
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antiporter
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5'-nucleotidase
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proton-pumping
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electrogenic
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vigna
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acpase
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diadenosine
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monophosphatase
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tripolyphosphate
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v-type
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diphosphonate
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ap4a
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chromatophores
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dihydrate
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tetraphosphate
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ectonucleotide
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exopolyphosphatase
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vacuolar-type
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radiata
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phosphomonoesterase
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autotaxin
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osmium
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pyrophosphate-dependent
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n,n'-dicyclohexylcarbodiimide
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decapping
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pyrophosphohydrolase
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sulfurylase
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molecular biology
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synthesis
- 3.6.1.1
- thiamine
- ppases
- vacuole
- apparatus
- nucleoside
-
tonoplast
- triphosphate
-
cytochemical
-
cisternae
- h+-atpase
- lysosome
- magnesium
- polyphosphate
- glucose-6-phosphatase
- orthophosphate
-
mung
- rubrum
-
cytochemistry
- rhodospirillum
- imidodiphosphate
-
saccule
-
nudix
-
h+-pumping
-
antiporter
- 5'-nucleotidase
-
proton-pumping
-
electrogenic
- vigna
- acpase
-
diadenosine
-
monophosphatase
- tripolyphosphate
-
v-type
- diphosphonate
- ap4a
-
chromatophores
-
dihydrate
- tetraphosphate
-
ectonucleotide
- exopolyphosphatase
-
vacuolar-type
- radiata
- phosphomonoesterase
- autotaxin
-
osmium
-
pyrophosphate-dependent
- n,n'-dicyclohexylcarbodiimide
-
decapping
-
pyrophosphohydrolase
-
sulfurylase
- molecular biology
- synthesis
Reaction
Synonyms
acid PPase, AT727_13205, AtPPA1, AtPPsPase1, BT2127, CBS-PPase, CBS-PPase1, chloroplast inorganic pyrophosphatase 1, class A type PPA, cobalt-dependent inorganic pyrophosphatase, CPE2055, cytosolic PPase, D1C enzyme, dhPPase, E-PPase, EcPpA, EcPPiase, ehPPase, family I inorganic pyrophosphatase, family I PPase, family I pyrophosphatase, family II inorganic pyrophosphatase, family II PPase, H+-PPase, H+-pyrophosphatase, H+-translocating/vacuolar inorganic pyrophosphatase, Hpp1 protein, HVO_0729, HvPPA, hyperthermophilic inorganic pyrophosphatase, inorganic diphosphatase, inorganic PPase, inorganic pyrophosphatase, inorganic pyrophosphatase 1, inorganic pyrophosphatase-like protein, inorganic pyrophosphorylase, IPP, IPP1, Ipp1p, IPPase, LHPPase, M-PPase, manganese-dependent inorganic pyrophosphatase, MazG, MdPPa, membrane-integral inorganic pyrophosphatase, membrane-integral pyrophosphatase, miPPase, mitochondrial pyrophosphatase, Mn2+-bound canonical Family II PPase, More, Mtb PPiase, Mthe_0236, MtPPA1, MtPPiase, nucleotide-regulated pyrophosphatase, OVP1, p26.1a, p26.1b, PfPPase, PH1907, Pho-PPase, phospholysine phosphohistidine inorganic pyrophosphate phosphatase, phosphoprotein p26.1, PPA, PPA1, PpaC, PPase, PPase 1, PPase 2, ppase-1, PPase-2, PPase1, PPase2, PPase4, PPias, PPIase, proton-translocating inorganic pyrophosphatase, PYP-1, pyrophosphatase, pyrophosphatase, inorganic, Pyrophosphate phospho-hydrolase, pyrophosphate phospho-hydrolase 1, Pyrophosphate phosphohydrolase, Pyrophosphate-energized inorganic pyrophosphatase, RmPPase, Rv3628, siPPiase, soluble inorganic pyrophosphatase, soluble inorganic pyrophosphatase 2, soluble pyrophosphatase, soluble-type yeast PPase, sPPAse, ST2226, Tc-sPPase, TC004566, TcasGA2_TC004566, TgPPase, ThPP1, Tm-PPase, TM0913, V-PPase, vacuolar H(+)-PPase, vacuolar H(+)-pyrophosphatase, vacuolar H+-pyrophosphatase, vacuolar H+-translocating inorganic pyrophosphatase, vacuolar H+-translocating pyrophosphatase, vacuolar pyrophosphatase, VHP, VP1, VSP, VVPP1
ECTree
3.6.1.1 inorganic diphosphataseAdvanced search results
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results (Engineering
Engineering on EC 3.6.1.1 - inorganic diphosphatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H98Q
the mutant shows highly reduced activity compared to the wild-type enzyme, crystal structure determination and comparison of substrate/inhibitor binding to the wild-type enzyme
E47Q
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
H23A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20K
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20L
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
N172A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
S115A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
S80A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T113A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T50A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20L
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
-
N312S
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
R276A
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency compared to wild-type, negative co-operativity is retained in the R276A variant in the presence of mononucleotides but is reversed by diadenosine tetraphosphate. The R276A substitution abolishes activation by ATP and diadenosine tetraphosphate, while preserving the ability to bind them
R276E
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type
R276K
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type
N312S
D102N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D26A
D42E
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
D65N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D67N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D70N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D97E
E145Q
E20D
E31A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
E31D
H136Q
H140Q
-
variant can be dissociated in trimers, hydrolytic activity 110% of wild-type enzyme
K112Q
K112Q/K115A
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site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K112Q/K148Q
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site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K115A
K148Q
R43Q
Y141F
-
22% relative activity compared to wild type enzyme, decreased thermostability compared to wild type
Y51F
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64% relative activity compared to wild type enzyme, thermostability as wild type
Y55F
S213N
C16S
site-directed mutagenesis, the mutant shows a loss of 50% activity and a reduction in sensitivity to reductants and oxidized glutathione compared to the wild-type enzyme. In addition, the replacement causes a considerable disruption in thermostability, C16S substitution destabilizes PPase through impairing trimer-trimer interactions
Y140F
site-directed mutagenesis, the mutant shows 78% reduced activity compared to the wild-type enzyme
Y169A
-
site-directed mutagenesis of the CBS domain residue, the mutant shows altered kinetics with adenine nucleotides compared to the wild-type enzyme
D54N
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
D57N
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to wild-type
D89N
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to wild-type
D198N
site-directed mutagenesis, the mutant shows 5fold reduced kcat compared to wild-type
D203N
site-directed mutagenesis, the mutant shows 600fold reduced activity compared to wild-type
D235N
site-directed mutagenesis, the mutant shows 6fold reduced kcat compared to wild-type
K136R
site-directed mutagenesis, the mutant shows a 40fold increased Km for diphosphate compared to wild-type
R158K
site-directed mutagenesis, the mutant shows a moderately altered kcat and Km for diphosphate compared to wild-type
D115E
site-directed mutagenesis, the mutation affects metal binding and the hydrogen bonding network in the active, in contrary to the wild-type enzyme, the mutant shows an open conformation variant of the hitherto unobserved two-phosphate and two bridging water active site, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D117E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D120E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D120N
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D152E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
E48D
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
Y93F
R295A
G190A
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
G190W
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
I259V
site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme
I260D
site-directed mutagenesis, the mutant shows 86% reduced activity compared to the wild-type enzyme
I260E
site-directed mutagenesis, the mutant shows 89% reduced activity compared to the wild-type enzyme
I260V
site-directed mutagenesis, the mutant shows 20% increased activity compared to the wild-type enzyme, the mutant is activable by NaF in contrast to the wild-type enzyme
T191G
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
G190A
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
-
G190W
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
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I259V
-
site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme
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I260D
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site-directed mutagenesis, the mutant shows 86% reduced activity compared to the wild-type enzyme
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I260E
-
site-directed mutagenesis, the mutant shows 89% reduced activity compared to the wild-type enzyme
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T191G
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
-
D169A
mutant enzyme shows 1.8% of wild-type pyrophosphatase activity
G163A
mutant enzyme shows 3.1% of wild-type pyrophosphatase activity
H125A
mutant enzyme shows 7.5% of wild-type pyrophosphatase activity
H165A
mutant enzyme shows 0.4% of wild-type pyrophosphatase activity
P103A
mutant enzyme shows 3.3% of wild-type pyrophosphatase activity
P122A
mutant enzyme shows 8.0% of wild-type pyrophosphatase activity
P167A
mutant enzyme shows 1.8% of wild-type pyrophosphatase activity
R159A
mutant enzyme shows 1.1% of wild-type pyrophosphatase activity
S123A
mutant enzyme shows 16% of wild-type pyrophosphatase activity
S158A
mutant enzyme shows 2.0% of wild-type pyrophosphatase activity
G119A
the mutant shows less than 50% activity towards diphosphate and increased activity towards ATP compared to the wild type enzyme
G119S
the mutant shows about 140% activity towards diphosphate and increased activity towards ATP and dATP compared to the wild type enzyme
D190A
the Na+ dose dependency of the D190A variant closely resembles that of the wild-type enzyme
D703N
the variant exhibits a much lower slope on the rate vs [Na+] plot than the wild-type enzyme at all of the K+ concentrations examined
E41Q/E42Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
E45Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
E61Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
K118A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
R97A/R98A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
D190A
-
the Na+ dose dependency of the D190A variant closely resembles that of the wild-type enzyme
-
D703N
-
the variant exhibits a much lower slope on the rate vs [Na+] plot than the wild-type enzyme at all of the K+ concentrations examined
-
E41Q/E42Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
E45Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
E61Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
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K118A
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significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
R97A/R98A
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significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
A226S
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
A238S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E225A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F224A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
F240A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G221A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G222A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G229A
-
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
G231A
-
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
G233A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G234A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G241A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
I227A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
L223A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
L232A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L239A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
M237A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R242A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
S235A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
S236A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T228A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
Y230A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
N312S
-
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
-
N312S
-
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
-
D26A
-
site-directed mutagenesis, the mutant does not obey Michaelis-Menten kinetics
D26A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
D97E
-
decreased pH-independence rates of diphosphate hydrolysis and resynthesis, destabilized EMg2(Mgdiphosphate)2 complex, raised pKa, Mg2+ binding changed
E145Q
-
easy formation of dimers with 5% of activity of the corresponding hexamer, 5fold increase of Kd for Mg2+ at site 2, no inhibition with high concentrations of Mg2+
E145Q
-
site-directed mutagenesis, about 80% reduced activity and altered kinetic properties compared to the wild-type enzyme
H136Q
-
variant can be dissociated in trimers, hydrolytic activity 225% of wild-type enzyme
K112Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
K112Q
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K115A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
K115A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
K148Q
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
K148Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
R43Q
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R43Q
site-directed mutagenesis, crystal structure determination and analysis and comparison to the wild-type structure
R43Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
Y55F
-
7% relative activity compared to wild type enzyme, conformational change, thermostability as wild type
Y55F
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
S213N
site-directed mutagenesis, the substitution confers significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations. The catalytic constant decreases by a factor of 4.5 upon Ser213 replacement
S213N
Ethanoligenens harbinense UniProt
-
site-directed mutagenesis, the substitution confers significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations. The catalytic constant decreases by a factor of 4.5 upon Ser213 replacement
-
Y93F
site-directed mutagenesis, the mutation affects metal binding and the hydrogen bonding network in the active, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
additional information
construction of an N-truncated variant of AtPPA1 with residues 1-29 deleted (DELTA(1-29)) produced using construct pMCSG48-AtPPA1-DELTA(1-29)
additional information
-
construction of an N-truncated variant of AtPPA1 with residues 1-29 deleted (DELTA(1-29)) produced using construct pMCSG48-AtPPA1-DELTA(1-29)
additional information
construction of the vacuolar H+-translocating pyrophosphatase (H+-PPase) loss-of-function fugu5 mutant that is susceptible to drought and displays pleotropic postgerminative growth defects due to excess diphosphate. Specific removal of PPi from a fugu5 mutant background (i.e. in the pAVP1::IPP1 transgenic line) rescues all recognized developmental defects and vigorously enhances growth. The GC1 promoter is properly expressed in guard cells in the fugu5-1 background. Construction and phenotypic analyses of the pGC1::IPP1 line in the fugu5-1 background expressing the soluble PPase from Saccharomyces cerevisiae strain 288c. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype, phenotypes, overview
additional information
-
PPase gene silencing by RNA interference, RNAi-mediated gene disruption suppressed native protein expression and mRNA levels in worm lung-stage larvae, recombinant AsPPase-immunized mice are protected from migration of challenge Ascaris suum larvae through the lungs
additional information
isolation of pyp-1 deletion mutant, a constructed null mutant of pyp-1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function, phenotype, overview
additional information
-
isolation of pyp-1 deletion mutant, a constructed null mutant of pyp-1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function, phenotype, overview
additional information
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
additional information
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
additional information
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
additional information
-
several mutants described that have minor effects on the binding of metal ions or diphosphate
additional information
-
metabolic profiling, sugar content of transgenic Arabidopsis thaliana plants expressing the Escherichia coli enzyme, the level of free phosphate in the leaves of transgenic plants is increased 2-3fold, and the UDP-glucose level is increased 2-6fold, but neither sucrose nor glucose levels as well as triphosphate level are unaltered, the photosynthetic activity of the mutants is reduced by 20-40% due to phosphate accumulation, overview
additional information
-
construction of a modified variant of wild type PPase with a derivative of ATP chemically attached to the amino group of Lys146
additional information
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
additional information
Ethanoligenens harbinense UniProt
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
additional information
isolated soluble inorganic diphosphatase gene ThPP1 from Thellungiella halophila is transformed this gene into the Oryza sativa subsp. japonica cv. Kitaake to investigate the functional roles of the ThPP1 gene under saline-alkali stresses. Two independent transgenic lines of T3 generation are subjected to the alkali stress by NaHCO3 and Na2CO3, then the profiles of physiological changes and the transcriptome-based differentially expressions in the transgenic rice are evaluated. Rice transcriptome sequencing, phenotypes, overview. The transgenic rice shows beneficial physiological changes under alkali stress. The accumulations of sucrose and starch in the leaves of the transgenic lines are significantly higher than those of the wild-type rice plants
additional information
-
isolated soluble inorganic diphosphatase gene ThPP1 from Thellungiella halophila is transformed this gene into the Oryza sativa subsp. japonica cv. Kitaake to investigate the functional roles of the ThPP1 gene under saline-alkali stresses. Two independent transgenic lines of T3 generation are subjected to the alkali stress by NaHCO3 and Na2CO3, then the profiles of physiological changes and the transcriptome-based differentially expressions in the transgenic rice are evaluated. Rice transcriptome sequencing, phenotypes, overview. The transgenic rice shows beneficial physiological changes under alkali stress. The accumulations of sucrose and starch in the leaves of the transgenic lines are significantly higher than those of the wild-type rice plants
additional information
-
immobilization of the purified enzyme on hydrophobic supports polycephamide and lysopolycephamide allows preservation of 24.2% and 17.3% of the starting catalytic activities with activity of imMobilized enzymes per gram support of 507 and 285 U/g, respectively
additional information
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
-
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
MdVHP1 overexpression in apple shoot culture, phenotypes, overview
additional information
-
MdVHP1 overexpression in apple shoot culture, phenotypes, overview
additional information
construction of the truncated version of MtPPA1-DELTA(1-30), which is not possible to express
additional information
-
construction of the truncated version of MtPPA1-DELTA(1-30), which is not possible to express
additional information
OVP1 overexpression in rice seedlings, phenotypes, overview
additional information
-
OVP1 overexpression in rice seedlings, phenotypes, overview
additional information
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
additional information
-
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
additional information
-
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
-
additional information
construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
additional information
-
construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
additional information
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construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
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additional information
knockdown of Tc-SPPase in the genome of Tribolium castaneum via pRNAi. Injection of Tc-sPPase dsRNA completely inhibits its expression when compared to the control, confirming that Tc-sPPase transcription is largely reduced
additional information
-
knockdown of Tc-SPPase in the genome of Tribolium castaneum via pRNAi. Injection of Tc-sPPase dsRNA completely inhibits its expression when compared to the control, confirming that Tc-sPPase transcription is largely reduced
