Information on EC 1.1.3.17 - choline oxidase

-

Substrates: -
Products: -

?

3,3-dimethyl-butanol + O2

3,3-dimethylbutanal + H2O2

-

Substrates: -
Products: -

?

3,3-dimethylbutan-1-ol + 2 O2 + H2O2

?

Substrates: -
Products: -

?

3,3-dimethylbutan-1-ol + O2

?

-

672121, 671605

Substrates: 10fold lower activity compared to choline
Products: -

?

3-(dimethylamino)propan-1-ol + 2 O2 + H2O

? + 2 H2O2

-

Substrates: -
Products: -

?

3-hydroxypropyl-trimethylamine + 2 O2 + H2O2

?

724108

Substrates: -
Products: -

?

3-trimethylamino-1-propanol + 2 O2 + H2O

3-trimethylaminopropanoate + 2 H2O2

-

Substrates: -
Products: -

?

4-trimethylamino-1-butanol + 2 O2 + H2O

4-trimethylaminobutanoate + 2 H2O2

-

Substrates: -
Products: -

?

betaine aldehyde + O2 + H2O

betaine + H2O2

13 entries

betaine aldehyde + O2 + H2O

glycine betaine + H2O2

739787, 740068, 741453, 740986

Substrates: -
Products: -

?

choline + 2 O2 + H2O

betaine + 2 H2O2

choline + 2 O2 + H2O2

betaine + 2 H2O2

choline + O2

betaine aldehyde + H2O2

36 entries

choline + O2 + H2O

betaine + 2 H2O2

Substrates: -
Products: -

?

diethanolamine + O2

?

-

Substrates: -
Products: -

?

diethylamino ethanol + 2 O2 + H2O2

? + 2 H2O2

diethylaminoethanol + 2 O2 + H2O

? + 2 H2O2

-

Substrates: -
Products: -

?

dimethylaminoethanol + 2 O2 + H2O

? + 2 H2O2

-

Substrates: -
Products: -

?

FADH2 + O2

FAD + H2O2

-

672121, 674159, 655800, 671605, 672136

Substrates: -
Products: -

?

glycine betaine + H2O2

betaine aldehyde + O2 + H2O

-

739846

Substrates: -
Products: -

?

monoethanolamine + O2

aminoacetaldehyde + H2O2

N,N-dimethylaminoethanol + O2

(dimethylamino)acetaldehyde + H2O2

N,N-dimethylethanolamine + O2

N,N-dimethylethanalamine + H2O2

-

Substrates: -
Products: -

?

N-methylethanolamine + O2

N-methylethanalamine + H2O2

-

Substrates: -
Products: -

?

triethanolamine + O2

?

tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2

? + 2 H2O2

additional information

?

-

7 entries

betaine aldehyde + O2 + H2O

betaine + H2O2

9 entries

betaine aldehyde + O2 + H2O

glycine betaine + H2O2

739787, 740068, 741453, 740986

Substrates: -
Products: -

?

choline + 2 O2 + H2O

betaine + 2 H2O2

choline + 2 O2 + H2O2

betaine + 2 H2O2

choline + O2

betaine aldehyde + H2O2

22 entries

FADH2 + O2

FAD + H2O2

-

672121, 674159, 655800, 671605, 672136

Substrates: -
Products: -

?

glycine betaine + H2O2

betaine aldehyde + O2 + H2O

-

739846

Substrates: -
Products: -

?

additional information

?

-

FAD

22 entries

FMN

the enzyme-bound flavin shows a progressive shift of the fluorescence excitation maximum (lambdaex) from 468 to 399 nm with increasing pH value between pH 6.0 and 10.0, consistent with a metastable photoinduced protein-flavin adduct. In contrast, the maximal lambdaem is independent of pH, with values of about 526 nm

763387

(2-amino-ethyl)trimethylammonim chloride

-

2-chloro-N-(2-chloroethyl)-N-methylethanamine

-

nitrogen mustard, strong competitive inhibitor

3,3-dimethylbutyraldehyde

-

product analogue inhibition, 74-90% reduced flavin reduction dependent on pH

672121

4-chloromercuribenzoate

-

75% inhibition at 1 mM

Ag+

-

AgNO3

-

allyltrimethylammonium chloride

-

Amytal

-

Betaine aldehyde

-

Cu2+

diethyldicarbonate

-

competitive inhibition, 10% inhibition

676916

diethylmethylamine

-

Dimethylamine

-

dimethylethylamine

-

ethylamine

-

ethylparathion

-

uncompetitive versus choline, inhibition and subsequent inactivation of the enzyme, active site specific

674036

glycine betaine

Hg2+

HgCl2

-

iodoacetic acid

-

10% inhibition at 1 mM

methylamine

-

methylethylamine

-

Mn2+

-

7% inhibition at 1 mM

N,N-dimethylglycine

-

N-methylglycine

-

Nicotine

P16101

ability of nicotine to inhibit catalytic activity of choline oxidase used for biosensorial detection of

686373

p-chloromercuribenzoate

-

paraoxon

-

uncompetitive versus choline, inhibition and subsequent inactivation of the enzyme, active site specific

674036

PMSF

-

uncompetitive inhibition, 50% inhibition

676916

Quinine

-

20% inhibition at 1 mM

rotenone

-

tetramethylamine

-

trimethylamine

-

trimethylethylammonium chloride

-

Zn2+

additional information

-

NAD+

-

stimulation of choline oxidation

1.01

3,3-dimethyl-1-butanol

-

pH 8.0, 25°C

0.11 - 8.7

Betaine aldehyde

7 entries

2.3 - 2.35

betaine-aldehyde

0.25 - 213

choline

37 entries

14

N,N-Dimethylaminoethanol

-

0.32

N,N-dimethylethanolamine

-

pH 8.0, 25°C

0.52

N-Methylethanolamine

-

pH 8.0, 25°C

0.006 - 703

O2

13 entries

additional information

14 entries

-

8

3,3-dimethyl-1-butanol

-

pH 8.0, 25°C

0.2 - 133

Betaine aldehyde

8 entries

1.71 - 11.6

betaine-aldehyde

0.02 - 86

choline

43 entries

5.9

N,N-dimethylethanolamine

-

pH 8.0, 25°C

0.37

N-Methylethanolamine

-

pH 8.0, 25°C

0.09 - 15

O2

additional information

overall turnover of mutant variant about 60-fold decreased with choline compared to wild-type enzyme

-

0.031 - 2

3,3-dimethylbutan-1-ol

0.38 - 99

Betaine aldehyde

0.00009 - 237

choline

19 entries

0.0049 - 203

O2

12 entries

additional information

kcat/Koxygen values are independent of the pH between pH 5.0 and 10.0, average value is 1.7 mM

-

9

(2-amino-ethyl)trimethylammonim chloride

-

pH 8.0, 25°C

15

allyltrimethylammonium chloride

-

pH 8.0, 25°C

2

Betaine aldehyde

-

oxidation of choline is competitively inhibited

5

diethylmethylamine

-

pH 8.0, 25°C

6

Dimethylamine

-

pH 8.0, 25°C

9

dimethylethylamine

-

pH 8.0, 25°C

11

ethylamine

-

pH 8.0, 25°C

15

glycine betaine

-

pH 8.0, 25°C

26

methylamine

-

pH 8.0, 25°C

8

methylethylamine

-

pH 8.0, 25°C

57

N,N-dimethylglycine

-

pH 8.0, 25°C

405

N-methylglycine

-

pH 8.0, 25°C

11

tetramethylamine

-

pH 8.0, 25°C

2.4

trimethylamine

-

pH 8.0, 25°C

13

trimethylethylammonium chloride

-

pH 8.0, 25°C

additional information

-

inhibition kinetics

-

0.034

wild-type, substrate triethanolamine, 30°C, pH 8

0.08

H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system

0.09

mutant S101A/D250G/F253R/V355T/F357R/M359R, substrate choline, 30°C, pH 8

0.28

apparent, H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system

0.3

10.6

wild-type, substrate choline, 30°C, pH 8

12.5

-

lyophilized powder

12.8

-

gel filtration

32.1

-

purified enzyme, pH 10.0, 25°C

7.57

-

389717

additional information

10 entries

10

7

7 - 10

-

assay at

7 - 8

-

choline as substrate

7 - 9

-

assay at

724368

7.5

-

8

8 - 11

H99N mutant

9

9.5

-

assay at

5 - 10

5.5 - 10

-

6

4°C, the anionic flavosemiquinone is slowly oxidized under aerobic conditions

696242

6 - 10

6 - 8

H99N mutant, lower KM compared to pH 8-11. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system

6.5 - 9.6

pH effects on the rate constants for fast transition from inactive to active form measured, choline concentrations in the range from 0.1 to 10 mM, temperature effects on enzyme reactivation determined at pH 6

7.5 - 10

P16101

biosensor retains 60% of its maximum response

686373

8

the anionic flavosemiquinone of choline oxidase is unusually insensitive to both molecular oxygen and artificial electron acceptors

696242

8 - 11

H99N mutant, no impact on KM, highest KM. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system

9 - 10

-

additional information

22

-

assay at

25

35 - 40

-

37

-

assay at

40

-

10 - 45

monitoring initial rates of oxygen consumption with oxygen electrode thermostated at, 0.2 mM oxygen in 50 mM sodium pyrophosphate, pH 8

685162

18 - 30

P16101

similar to that of the free enzyme ranging between 25°C and 35°C

686373

20 - 39

effect of temperature on the rate of reactivation at pH 6

5 - 9

-

the enzyme is irreversibly inactivated in acidic media at pH of less than 4.0

740937

additional information

4.1

Achromobacter cholinophagum

-

isoelectric focusing

740932

-

389717

-

Arthrobacter globiformis ATCC 8010

17 entries

-

724368

-

Cylindrocarpon didymum M-1

M-1

389717, 389719, 389721, 389723

-

M-1

389717, 389719, 389721, 389723

-

-

-

Fusarium oxysporum V2

-

-

gene codA

-

Sinorhizobium meliloti

102F34

Sinorhizobium meliloti 102F34

-

102F34

-

cv. Superior, wild-type and transgenic plants expressing bacterial choline oxidase (codA) gene of Arthrobacter globiformis

-

-

commercial preparation

leaf

-

transgenic and wild-type

-

additional information

chloroplast

-

glycine betaine production in transgenic plants

-

membrane-bound

5739

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

evolution

malfunction

-

replacing Asn510 with alanine or histidine negatively affects both the reductive and oxidative half-reactions catalyzed by choline oxidase. Substitution of Asn510 with alanine, but not with histidine, results in a change from stepwise to concerted mechanisms for the cleavages of the OH and CH bonds of choline catalyzed by the enzyme

metabolism

physiological function

additional information

117000 - 122000

gel filtration

120000

128000

-

gel filtration

145000

-

sedimentation velocity method of Svedberg and Pederson

59000

-

PAGE

389718

60612

2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence

654364

60614

2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence

654364

64000

66000

71000

-

SDS-PAGE

72000

83000

-

gel filtration

?

-

x * 66000, SDS-PAGE

dimer

homodimer

monomer

additional information

-

proposed catalytic base is H466

654876

active site of wild-type choline oxidase, resolution of 1.86 A

anaylsis of biophysical properties of choline oxidase

696242

crystal structure determined by synchrotron X-ray radiation, refined to a resolution of 1.86 A, data collected at 100 K

hanging drop vapor diffusion method, 1.2-1.8 M ammonium sulfate and 10% (v/v) DMSO in 0.1 M Bis-Tris propane (pH 8.5), flash-frozen in liquid nitrogen. Analysis of the flavin C4a-oxygen adduct in choline oxidase

696349

in complex with glycine betaine, hanging drop vapor diffusion method, using 0.1 M magnesium acetate pH 6.0, 50 mM calcium chloride, 2.5% (v/v) glycerol, 10% (w/v) PEG 6000

739787

mutant enzyme S101A, hanging drop vapor diffusion method, using 80 mM sodium cacodylate, 20% (v/v) PEG6000, 20% (v/v) glycerol, 150 mM Mg-acetate at pH 6.0

711016

purified recombinnat wild-type enzyme and mutant V464A, hanging drop vapor diffusion, room temperature, from 10-15% v/v PEG 6000, 50-200 mM magnesium acetate, 200 mM trimethylamine, and 0.08 M sodium cacodylate, pH 6.0, X-ray diffraction structure determination and analysis at 2.2 A resolution

E312A

generated for investigation of the negative charge on Glu312, enzyme inactive

E312D

E312Q

generated for investigation of the negative charge on Glu312, Kd value for choline about 500times larger than that of wild-type

F357A

the mutant shows about 240fold reduced catalytic efficiency compared to the wild type enzyme

740077

H351A

generated by site-directed mutagenesis

H351Q

the kcat and kcat/Km values of the H351Q emutant in atmospheric oxygen are 45 and 5000fold lower than those of the wild type enzyme, respectively

740068

H466A

H466D

-

site-directed mutagenesis, the mutation alters the flavin binding to the enzyme, while substrate choline is normally bound, binding og glycine btaine is inhibited, spectrometrical analysis, the mutant shows a different flavin-binding stoichiometry of 0.29:1, compared to 1:1 for the wild-type enzyme, stabilized at pH 6.0-10.0, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466A and the wild-type enzyme, the mutant shows no catalytic activity

672136

H466Q

H99N

mutant, analysis of kinetic parameters

M359R

mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13

M62A

the mutant shows about 3fold reduced catalytic efficiency compared to the wild type enzyme

740077

M62A/F357A

the enzyme shows a lack of the isomerization detected in wild type choline oxidase, and a lack of saturation with an oxygen concentration as high as 1 mM, while most other kinetic parameters are similar to those of wild type choline oxidase

740077

N510A

-

site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, enzyme kinetics decrease of 4300fold in the kcat/Kcholine, 600fold in the kred, 660fold in the kcat, and 50fold in the kcat/Koxygen values

N510D

-

site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, 75% of the flavin associates noncovalently, inactive mutant

N510H

-

site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, decreases in the kcat/Kcholine, the kred, the kcat, and the kcat/Koxygen values

N510L

-

site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein

S101A

S101A/D250G/F253R/V355T/F357R/M359R

mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13, with a 20fold increased kcat compared to that of the wildtype enzyme. This variant enables the oxidation of 10 mM hexanol to hexanal in less than 24h with 100% conversion and catalyzes significantly improved oxidation of saturated, unsaturated, aliphatic, cyclic and benzylic alcohols

S101A/V355T/F357R

mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13

S101A/V355T/F357R/M359R

mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13

S101C

S101T

S101V

contrary to wild-type, stopped-flow traces for the reductive half-reaction are biphasic, corresponding to the reactions of proton abstraction and hydride transfer. The rate constants for proton transfer in the S101T/C/V variants decrease logarithmically with increasing hydrophobicity of residue 101

762669

V355T/F357R

mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13

V464A

V464T

A21V

-

site-directed mutagenesis in the FAD binding site

A21V/G62D

-

site-directed mutagenesis, the mutant shows 1.93fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and slightly reduced activity with choline compared to the wild-type enzyme

A21V/G62D/I69V

-

site-directed mutagenesis, the mutant shows 1.68fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme

A21V/G62D/I69V/S348L

-

site-directed mutagenesis, the mutant shows 3.45fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme

A21V/G62D/S348C

-

site-directed mutagenesis, the mutant shows 5.18fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme

A21V/G62D/S348L

-

site-directed mutagenesis, the mutant shows 3.72fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme

A21V/G62D/S348L/V349L

-

site-directed mutagenesis, the mutant shows 5.75fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme

A21V/K394R

-

site-directed mutagenesis, the mutant shows 85% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme

F351Y

-

site-directed mutagenesis in the substrate binding site, the mutant shows reduced activity with choline compared to the wild-type enzyme

G62D

-

site-directed mutagenesis in the FAD binding site, the mutant shows 2fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme

G62D/F351Y

-

site-directed mutagenesis, the mutant shows 2.14fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme

G62D/R249H/F351Y

-

site-directed mutagenesis, the mutant shows 2.7fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme

I69V

-

site-directed mutagenesis in the FAD binding site, the mutant shows93% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme

P393Q/S530G

-

site-directed mutagenesis, the mutant shows 1.5fold increased activity with choline compared to the wild-type enzyme

S348L

-

site-directed mutagenesis in the substrate binding site

T116I/K128M

-

site-directed mutagenesis, the mutant shows unaltered activity with choline compared to the wild-type enzyme

T116I/K128M/P393Q/S530G

-

site-directed mutagenesis, the mutant shows 2.32fold increased activity with choline compared to the wild-type enzyme

V349L

-

site-directed mutagenesis in the substrate binding site

A21V

-

site-directed mutagenesis in the FAD binding site

-

G62D

-

site-directed mutagenesis in the FAD binding site, the mutant shows 2fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme

-

I69V

-

site-directed mutagenesis in the FAD binding site, the mutant shows93% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme

-

S348L

-

site-directed mutagenesis in the substrate binding site

-

V349L

-

site-directed mutagenesis in the substrate binding site

-

additional information

3 - 6

-

inactivation takes place at both 27°C and 37°C

695307

6 - 9

-

inactivation takes place at both 27°C and 37°C

695307

7 - 8.5

-

no significant inactivation at both 27°C and 37°C

695307

7 - 9

-

50% initial activity is lost at 40°C at pH 6.0 and 9.5

8 - 10.2

-

purified enzyme, 30°C, 10 min, stable at

additional information

30

wild-type, stable for at least 3 h

32

melting temperature of wild-type

40

mutant S101A/V355T/F357R/M359R, 3 h, 10% residual activity. Mutant S101A/D250G/F253R/V355T/F357R/M359R, 3 h, almost 50% residual activity

40 - 45

-

incubated for 10 min at pH 8.5 and 40°C 20% initial activity is lost, 96% at 45°C, only 10% initial activity is lost at 45°C in presence of 10% glycerol

52

metling temperature of mutant S101A/D250G/F253R/V355T/F357R/M359R

70 - 90

-

no degradation when incubated for 1 h

698402

additional information

storage at -20°C and pH 6 results in a change in the conformation, loss of catalytic activity at pH 6, reactivation of the enzyme slow at pH 6 and temperatures between 20 and 39°C, facilitated by elevated pH values at 25°C and pH above 6.5

-

native enzyme 41fold by ammonium sulfate fractionation, gel filtation, anion exchange and hydroxyapatite chromatgraphy, and again gel filtration

-

purified with the bound flavin cofactor in the fully oxidized state

recombinant enzyme partially from stressed and non-stressed transgenic rice plant leaves by ammonium sulfate fractionation and desalting gel filtration

-

675130

recombinant enzyme, expression in Escherichia coli

654364

recombinant protein

685162

recombinant protein, purified to homogeneity, gel filtration

recombinant wild-type and mutants from Escherichia coli strain Rosetta(DE3)pLysS

recombinant wild-type enzyme in oxidized state to homogeneity

-

wild-type and mutant protein, purified enzymes have 50-70% of the enzyme-bound flavin cofactor as an air-stable anionic flavosemiquinone, converts slowly to oxidized state by extensive dialysis at pH 6 and 4°C

wild-type and mutant variants

Arabidopsis thaliana transformed with codA gene from Arthrobacter globiformis which encodes choline oxidase

-

389727

Balb/c mice used for toxicity studies of choline oxidase - no significant difference from control in terms of growth, body weight, food consumption, and blood biochemical indices. Analysis of various tissues show no significant effect

-

698402

choline oxidase from Arthrobacter pascens facilitates adaptation to osmotic stress in Escherichia coli

-

cloning of Sinorhizobium meliloti bet genes, Tn5 mutant LtS23-1020 is completed by plasmid pCHO34

Sinorhizobium meliloti

-

codA gene introduced into Synecochoccus sp. PCC 7942 and Arabidopsis thaliana leads to accumulation of glycinebetaine and enhanced tolerance to salt and cold stress, rice Oryza sativa L. genetically engineered, Agrobacterium-mediated transformation, ability to synthesize glycinebetaine is established by introducing the codA gene for choline oxidase from Arthrobacter globiformis

-

389724

expressed in Escherichia coli from plasmid pET/codA1

685162

expressed in Escherichia coli Rosetta(DE3)pLysS cells

expressed in Escherichia coli, plant expression vector pGAH/codA,codA gene and nos terminator fragments excised from pGAH/codA, ligated to stress-inducible SWPA2 promoter, fused into pCAMBIA3300 binary vector, resulting pScodA transformed into Solanum tuberosum by using Agrobacterium tumefaciens strain AGL0

-

689522

expressed in Escherichia coli, plasmid pET/codA1

expressed in Escherichia coli, strain Rosetta(DE3)pLysS, pET/codAmg plasmid, wild-type and Glu312 variants generated by site-directed mutagenesis

expressed in Escherichia coli, wild-type and H351A variant, plasmid pET/codAmg1-H351A

expressed in Eucalyptus globulus

741133, 740986

expression of wild-type and mutant enzymes in Escherichia coli

-

expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS

-

expression of wild-type and mutants in Escherichia coli strain Rosetta(DE3)pLysS

gene codA, expression in Euccalyptus globulus via Agrobaccterium tumefaciens strain EHA105 transfection method using vectors pBI121 and pGW23codA

-

726150

gene codA, expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold

-

heterologous expression in Escherichia coli DH5 alpha and BL21(DE3), respectively. Systematic exchange of individual segments of the Arthrobacter pascens gene with segments from a choline oxidase-encoding gene from Arthrobacter globiformis yielding a functional chimeric enzyme

-

695812

mutant enzyme S101A is expressed in Escherichia coli Rosetta(DE3)pLysS cells

711016

overexpression of the enzyme, fused to a chloroplast-transit peptide from Pisum sativum, in transgenic Oryza sativa plants using the Agrobacterium tumefaciens transfection system

-

675130

recombinant expression in Escherichia coli

696243, 696349

recombinant expression in Escherichia coli strain Rosetta (DE3)pLysS

conformational change reverting the enzyme to the native form, rate of approaching steady state independent of concentrations of choline and enzyme, increased to a limiting value with increasing pH

fully oxidized form of the enzyme is obtained via slow oxidation of the flavosemiquinone by extensive dialysis at pH 6 and 4°C

696243

Systematic exchange of individual segments of the Arthrobacter pascens gene with segments from a choline oxidase-encoding gene from Arthrobacter globiformis yielding a functional chimeric enzyme when produced in Escherichia coli

-

agriculture

analysis

biotechnology

nutrition

-

introducing of the codA gene into a cereal crop allows the biosynthesis of glycinebetaine

389724

synthesis