print visible entries

print all entries

Ligand pyridoxal

Basic Ligand Information

Molecular Structure

Related pathways

Show all BRENDA pathways known for pyridoxal

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

top print hide

Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.107

pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+

80781, 667329, 688568, 721873

-

1.2.3.8

pyridoxal + H2O + O2 = 4-pyridoxate + ?

740812

-

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641423, 641422, 641420, 641429, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 737378, 737622, 737767, 737809, 738236, 760178, 758844, 759126, 759183, 759342, 759346, 759093

1TD2, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641423, 641422, 641420, 641429, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 737378, 737622, 737767, 737809, 738236, 760178, 758844, 759126, 759183, 759342, 759346, 759093

2DDW, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641423, 641422, 641420, 641429, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 737378, 737622, 737767, 737809, 738236, 760178, 758844, 759126, 759183, 759342, 759346, 759093

3FHX, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641423, 641422, 641420, 641429, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 737378, 737622, 737767, 737809, 738236, 760178, 758844, 759126, 759183, 759342, 759346, 759093

4C5L, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641423, 641422, 641420, 641429, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 737378, 737622, 737767, 737809, 738236, 760178, 758844, 759126, 759183, 759342, 759346, 759093

6SU9, 3D-view

2.7.1.35

5 entries

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

top print hide

Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.65

pyridoxine + NADP+ = pyridoxal + NADPH

- , 287235

-

1.1.3.12

pyridoxine + O2 = pyridoxal + H2O2

-

-

2.6.1.30

pyridoxamine + pyruvate = pyridoxal + L-alanine

639958, 639957, 639959, 639960, 639956, -

2Z9W, 3D-view

2.6.1.30

pyridoxamine + pyruvate = pyridoxal + L-alanine

639958, 639957, 639959, 639960, 639956, -

2Z9X, 3D-view

2.6.1.30

2 entries

2.6.1.31

pyridoxamine + oxaloacetate = pyridoxal + L-aspartate

639961, -

-

3.1.3.1

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

651458

-

3.1.3.74

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

pyridoxal 5'phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

pyridoxal-5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

3 entries

Substrate in Enzyme-catalyzed Reactions (19 results)

top print hide

Show Substrate (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.107

pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+

80781, 655029, 656239, 667329, 688568, 699047, 710764, 721873

-

1.1.1.107

pyridoxal + NADP+ = 4-pyridoxolactone + NADPH + H+

655029, 656239

-

1.1.1.107

2 entries

1.1.1.2

pyridoxal + NADPH = 4,5-bis(hydroxymethyl)-2-methylpyridin-3-ol + NADP+

286165

-

1.1.99.9

pyridoxal + acceptor = 3-hydroxy-2-methylpyridine-4,5-dicarbaldehyde + reduced acceptor

287852

-

1.2.3.1

pyridoxal + H2O + O2 = 4-pyridoxic acid + H2O2

390415, 691701

-

1.2.3.8

pyridoxal + H2O + O2 = 4-pyridoxate + ?

390406, 390445, 390446, 390447, 740812

-

2.6.1.30

pyridoxal + L-alanine = pyridoxamine + pyruvate

739366

2Z9W, 3D-view

2.6.1.30

pyridoxal + L-alanine = pyridoxamine + pyruvate

739366

2Z9X, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641403, 641404, 641423, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 391873, 641409, 641418, 641429, 641405, 641411, 641414, 641410, 641412, 641413, 641417, 641419, 641420, 641421, 641427, 641426, 641422, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 671140, 675407, 672438, 673580, 675693, 677029, 723578, 723219, 723449, 722183, 737378, 737622, 737767, 737809, 738236, 738451, 702038, 760178, 758844, 759126, 759183, 759342, 759346, 759093

1TD2, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641403, 641404, 641423, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 391873, 641409, 641418, 641429, 641405, 641411, 641414, 641410, 641412, 641413, 641417, 641419, 641420, 641421, 641427, 641426, 641422, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 671140, 675407, 672438, 673580, 675693, 677029, 723578, 723219, 723449, 722183, 737378, 737622, 737767, 737809, 738236, 738451, 702038, 760178, 758844, 759126, 759183, 759342, 759346, 759093

2DDW, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641403, 641404, 641423, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 391873, 641409, 641418, 641429, 641405, 641411, 641414, 641410, 641412, 641413, 641417, 641419, 641420, 641421, 641427, 641426, 641422, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 671140, 675407, 672438, 673580, 675693, 677029, 723578, 723219, 723449, 722183, 737378, 737622, 737767, 737809, 738236, 738451, 702038, 760178, 758844, 759126, 759183, 759342, 759346, 759093

3FHX, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641403, 641404, 641423, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 391873, 641409, 641418, 641429, 641405, 641411, 641414, 641410, 641412, 641413, 641417, 641419, 641420, 641421, 641427, 641426, 641422, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 671140, 675407, 672438, 673580, 675693, 677029, 723578, 723219, 723449, 722183, 737378, 737622, 737767, 737809, 738236, 738451, 702038, 760178, 758844, 759126, 759183, 759342, 759346, 759093

4C5L, 3D-view

2.7.1.35

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641403, 641404, 641423, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 391873, 641409, 641418, 641429, 641405, 641411, 641414, 641410, 641412, 641413, 641417, 641419, 641420, 641421, 641427, 641426, 641422, 662055, 663303, 662961, 662200, 662007, 662402, 662440, 671140, 675407, 672438, 673580, 675693, 677029, 723578, 723219, 723449, 722183, 737378, 737622, 737767, 737809, 738236, 738451, 702038, 760178, 758844, 759126, 759183, 759342, 759346, 759093

6SU9, 3D-view

2.7.1.35

pyridoxal + ATP = pyridoxal 5'-phosphate + ADP

706419, 702038

1TD2, 3D-view

2.7.1.35

pyridoxal + ATP = pyridoxal 5'-phosphate + ADP

706419, 702038

2DDW, 3D-view

2.7.1.35

pyridoxal + ATP = pyridoxal 5'-phosphate + ADP

706419, 702038

3FHX, 3D-view

2.7.1.35

pyridoxal + ATP = pyridoxal 5'-phosphate + ADP

706419, 702038

4C5L, 3D-view

2.7.1.35

pyridoxal + ATP = pyridoxal 5'-phosphate + ADP

706419, 702038

6SU9, 3D-view

2.6.1.30

2 entries

2.7.1.35

10 entries

2.7.1.49

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate

641658, 738451

-

Product in Enzyme-catalyzed Reactions (22 results)

top print hide

Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.65

pyridoxine + NADP+ = pyridoxal + NADPH

- , 287235

-

1.1.3.12

pyridoxine + 2,6-dichloroindophenol = pyridoxal + ?

-

-

1.1.3.12

pyridoxine + O2 = pyridoxal + H2O2

287851, -

-

1.1.3.12

pyridoxine + vitamin K3 = pyridoxal + ?

-

-

2.6.1.30

pyridoxamine + 2-oxobutyrate = pyridoxal + (S)-2-aminobutyrate

-

2Z9W, 3D-view

2.6.1.30

pyridoxamine + 2-oxobutyrate = pyridoxal + (S)-2-aminobutyrate

-

2Z9X, 3D-view

2.6.1.30

pyridoxamine + 2-oxoglutarate = pyridoxal + L-glutamate

-

2Z9W, 3D-view

2.6.1.30

pyridoxamine + 2-oxoglutarate = pyridoxal + L-glutamate

-

2Z9X, 3D-view

2.6.1.30

pyridoxamine + pyruvate = pyridoxal + L-alanine

639958, 639957, 639959, 639960, 639956, -

2Z9W, 3D-view

2.6.1.30

pyridoxamine + pyruvate = pyridoxal + L-alanine

639958, 639957, 639959, 639960, 639956, -

2Z9X, 3D-view

1.1.3.12

3 entries

2.6.1.30

6 entries

2.6.1.31

pyridoxamine + oxaloacetate = pyridoxal + L-aspartate

639961, -

-

2.6.1.54

pyridoxamine + 2-oxoglutarate = pyridoxal + D-glutamate

637633

-

3.1.3.1

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

651458

-

3.1.3.18

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.2

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

651405, -

-

3.1.3.2

pyridoxyl 5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.2

2 entries

3.1.3.26

pyridoxal phosphate + H2O = pyridoxal + phosphate

651559, -

-

3.1.3.74

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

pyridoxal 5'phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

pyridoxal-5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.74

3 entries

3.1.3.75

pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate

-

-

3.1.3.8

pyridoxal phosphate + H2O = pyridoxal + phosphate

651559

-

Activator in Enzyme-catalyzed Reactions (6 results)

top print hide

Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.21

approx. 0.1 mM, 1.4fold increase in activity of isozyme A

390214

-

1.4.3.13

derivative

391736, 391740

-

1.4.3.13

needed for biosynthesis of the enzyme

391740

-

1.4.3.13

pyridoxal phosphate or closely related compound

391739

-

1.4.3.13

3 entries

4.1.1.14

weak activation

3969

-

4.4.1.13

is 23% as effective as pyridoxal 5'-phosphate

34693

-

Inhibitor in Enzyme-catalyzed Reactions (50 results)

top print hide

Show Inhibitors (50 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.107

substrate inhibition, 90% inhibition at 2 mM

655029

-

1.1.99.9

-

287852

-

1.14.13.9

less potent than pyridoxal phosphate

348531

-

1.17.1.4

Ki for 2-amino-4-hydroxypterine oxidation: 0.08 mM at 30 and 50°C, competitive; Ki for xanthine oxidation: 0.05 mM at 30°C, 0.11 mM at 50°C, competitive

644595

-

1.2.1.21

0.01 mM, 40% inhibition of total enzyme activity in cell extracts

390214

-

1.4.1.3

NADH and NADPH protect from inactivation

391601

-

2.3.1.263

-

702184

-

2.4.1.1

phosphorylase I, not II

488269

-

2.5.1.47

-

637331

-

2.5.1.49

inhibits the activity competitively with respect to pyridoxal 5'-phosphate

637331

-

2.7.1.35

-

641408, 737767

1TD2, 3D-view

2.7.1.35

-

641408, 737767

2DDW, 3D-view

2.7.1.35

-

641408, 737767

3FHX, 3D-view

2.7.1.35

-

641408, 737767

4C5L, 3D-view

2.7.1.35

-

641408, 737767

6SU9, 3D-view

2.7.1.35

0.1 mM, substrate inhibition

641426

1TD2, 3D-view

2.7.1.35

0.1 mM, substrate inhibition

641426

2DDW, 3D-view

2.7.1.35

0.1 mM, substrate inhibition

641426

3FHX, 3D-view

2.7.1.35

0.1 mM, substrate inhibition

641426

4C5L, 3D-view

2.7.1.35

0.1 mM, substrate inhibition

641426

6SU9, 3D-view

2.7.1.35

at high concentrations, substrate inhibition

759183

1TD2, 3D-view

2.7.1.35

at high concentrations, substrate inhibition

759183

2DDW, 3D-view

2.7.1.35

at high concentrations, substrate inhibition

759183

3FHX, 3D-view

2.7.1.35

at high concentrations, substrate inhibition

759183

4C5L, 3D-view

2.7.1.35

at high concentrations, substrate inhibition

759183

6SU9, 3D-view

2.7.1.35

effective competitive inhibitor

641407

1TD2, 3D-view

2.7.1.35

effective competitive inhibitor

641407

2DDW, 3D-view

2.7.1.35

effective competitive inhibitor

641407

3FHX, 3D-view

2.7.1.35

effective competitive inhibitor

641407

4C5L, 3D-view

2.7.1.35

effective competitive inhibitor

641407

6SU9, 3D-view

2.7.1.35

substrate inhibition

737809

1TD2, 3D-view

2.7.1.35

substrate inhibition

737809

2DDW, 3D-view

2.7.1.35

substrate inhibition

737809

3FHX, 3D-view

2.7.1.35

substrate inhibition

737809

4C5L, 3D-view

2.7.1.35

substrate inhibition

737809

6SU9, 3D-view

2.7.1.35

25 entries

3.1.2.6

-

37432

-

3.1.3.2

1 mM, 20% residual activity, competitive

730629

-

3.1.3.74

weak, 11 mM, 50% inhibition of hydrolysis of pyridoxal 5’-phosphate or pyridoxine 5’-phosphate

655965

-

3.2.1.26

-

136067, 136102

-

3.2.1.26

1 mM, 15% inhibition

136087

-

3.2.1.26

1 mM, 65% inhibition of invertase I, 25% inhibition of invertase II

136110

-

3.2.1.26

invertase I is more than 2fold more resistant than invertase IIA and IIB

136125

-

3.2.1.26

4 entries

4.1.1.19

-

4080, 4086

-

4.1.1.36

-

4409, 4415

-

4.1.1.36

reversed by equimolar amount of semicarbazide

4407

-

4.1.1.36

2 entries

4.2.1.24

-

210711

-

4.4.1.13

12.5 mM, in presence of 12 mM L-cystine 12% inhibition, in presence of 1 mM L-cystine 37% inhibition

651551

-

4.4.1.35

2.5 mM, 63% residual activity

651551

-

4.4.1.5

-

37432

-

5.6.2.1

-

678498

-

3D Structure of Enzyme-Ligand-Complex (PDB) (7 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (7 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.6.1.30

2Z9W, 3D-view

2.6.1.30

2Z9X, 3D-view

2.7.1.35

1TD2, 3D-view

2.7.1.35

2DDW, 3D-view

2.7.1.35

3FHX, 3D-view

2.7.1.35

4C5L, 3D-view

2.7.1.35

6SU9, 3D-view

2.6.1.30

2 entries

2.7.1.35

5 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (39 results)

top print hide

Show Turnover Number (39 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.107

59.2

-

pH 8.0, 30°C

656239

1.1.1.107

149

-

30°C, pH 9.2

667329

1.1.1.107

149

-

pH 9.2, 30°C

667329

2.6.1.30

41

-

-

671864

2.6.1.30

41

-

30°C, pH 9.0

671864

2.7.1.35

0.015

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.03

-

D235A mutant protein

702038

2.7.1.35

0.032

-

pH 8, 37°C

662007

2.7.1.35

0.05

-

pH 6.5, 30°C

662440

2.7.1.35

0.073

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.107

-

pH 6.6, 37°C

759183

2.7.1.35

0.12

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.165

-

wild-type, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.35

0.23

-

D235N mutant protein

702038

2.7.1.35

0.23

-

in the presence of Na+, at pH 7.0 and 30°C

738236

2.7.1.35

0.328

-

mutant C214D, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.35

0.4

-

pH 7, 37°C, recombinant enzyme

641426

2.7.1.35

0.47

-

pH 7.3, 37°C recombinant mutant A243G

760178

2.7.1.35

0.48

-

wild-type protein

702038

2.7.1.35

0.5

-

with ZnATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.58

-

pH 7.3, 37°C recombinant mutant H246Q

760178

2.7.1.35

0.67

-

pH 7.3, 37°C recombinant mutant D87H

760178

2.7.1.35

0.8

-

with MgATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.97

-

pH 7.3, 37°C recombinant wild-type enzyme

760178

2.7.1.35

0.995

-

pH 6.2, 37°C

673580

2.7.1.35

1.12

-

pH 7.3, 37°C recombinant mutant V128I

760178

2.7.1.35

1.3

-

wild type enzyme, at pH 7.4 and 37°C

737622

2.7.1.35

1.35

-

in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C

722183

2.7.1.35

1.42

-

presence of 40 mM K+, pH 7.3, 37°C

677029

2.7.1.35

1.5

-

recombinant wild-type enzyme, pH 7.2, 37°C

759342

2.7.1.35

2

-

kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

2.3

-

kinase 1 with MgATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

3.2

-

at pH 6.5 and 37°C

737809

2.7.1.35

3.3

-

presence of 40 mM Na+, pH 7.3, 37°C

677029

2.7.1.35

4.7

-

mutant enzyme C124A, at pH 7.4 and 37°C

737622

2.7.1.35

6.08

-

in 70 mM potassium phosphate buffer, pH 6.2

673580

2.7.1.35

131

-

recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C

723219

2.7.1.49

0.165

-

wild-type, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.49

0.328

-

mutant C214D, pH not specified in the publication, temperature not specified in the publication

738451

1.1.1.107

3 entries

2.6.1.30

2 entries

2.7.1.35

32 entries

2.7.1.49

2 entries

K_M Value (56 results)

top print hide

Show KM Value (56 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.107

0.076

-

-

80781

1.1.1.107

0.091

-

30°C, pH 9.2

667329

1.1.1.107

0.091

-

pH 9.2, 30°C

667329

1.1.1.107

0.473

-

30°C, pH 8.0

655029

1.1.1.107

13

-

pH 8.0, 30°C

656239

1.1.1.65

0.9

-

-

287236

1.1.1.65

1.6

-

-

287235

1.1.1.107

5 entries

1.1.1.65

2 entries

1.2.3.8

0.028

-

-

390445

2.6.1.30

0.012

-

pH 8.9, 25°C

639957

2.6.1.30

0.059

-

-

671864

2.6.1.30

0.059

-

30°C, pH 9.0

671864

2.7.1.35

0.00122

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.00165

-

recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C

723219

2.7.1.35

0.0028

-

in 70 mM potassium phosphate buffer, pH 6.2

673580

2.7.1.35

0.01

-

in the presence of K+

677029

2.7.1.35

0.01

-

presence of 40 mM Na+, pH 7.3, 37°C

677029

2.7.1.35

0.0153

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.0216

-

in the presence of K+, at pH 7.0 and 30°C

738236

2.7.1.35

0.022

-

pH 7, 37°C

641426

2.7.1.35

0.024

-

wild-type protein

702038

2.7.1.35

0.025

-

pH 6, 37°C

641418

2.7.1.35

0.03

-

with MgATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.033

-

-

641406

2.7.1.35

0.037

-

mutant enzyme C124A, at pH 7.4 and 37°C

737622

2.7.1.35

0.038

-

pH 7, 37°C, recombinant enzyme

641426

2.7.1.35

0.038

-

recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C

723219

2.7.1.35

0.04

-

pH 6.5

641413, 641417

2.7.1.35

0.044

-

pH 6.6, 37°C

759183

2.7.1.35

0.0441

-

in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C

722183

2.7.1.35

0.047

-

pH 8, 37°C

662007

2.7.1.35

0.053

-

wild type enzyme, at pH 7.4 and 37°C

737622

2.7.1.35

0.058

-

D235N mutant protein

702038

2.7.1.35

0.0587

-

pH 6.2, 37°C

673580

2.7.1.35

0.07

-

pH 6.5, 30°C

662440

2.7.1.35

0.0739

-

in the presence of Na+, at pH 7.0 and 30°C

738236

2.7.1.35

0.075

-

in the presence of Na+

677029

2.7.1.35

0.075

-

presence of 40 mM Na+, pH 7.3, 37°C

677029

2.7.1.35

0.0909

-

recombinant enzyme, pH 7.5, 37°C

759346

2.7.1.35

0.097

-

pH 7, 37°C

641425

2.7.1.35

0.1

-

kinase 1 with MgATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.111

-

wild-type, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.35

0.141

-

pH 7.3, 37°C recombinant mutant H246Q

760178

2.7.1.35

0.17

-

D235A mutant protein

702038

2.7.1.35

0.177

-

pH 7.3, 37°C recombinant mutant A243G

760178

2.7.1.35

0.189

-

pH 7.3, 37°C recombinant wild-type enzyme

760178

2.7.1.35

0.19

-

37°C

391873

2.7.1.35

0.19

-

kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.24

-

recombinant wild-type enzyme, pH 7.2, 37°C

759342

2.7.1.35

0.26

-

mutant C214D, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.35

0.35

-

with ZnATP2- as substrate, pH 7.3, 37°C

663303

2.7.1.35

0.49

-

at pH 6.5 and 37°C

737809

2.7.1.35

2.09

-

pH 7.3, 37°C recombinant mutant D87H

760178

2.7.1.35

3.839

-

pH 7.3, 37°C recombinant mutant V128I

760178

2.7.1.49

0.111

-

wild-type, pH not specified in the publication, temperature not specified in the publication

738451

2.7.1.49

0.24

-

pH 6.2, 37°C

641658

2.7.1.49

0.26

-

mutant C214D, pH not specified in the publication, temperature not specified in the publication

738451

2.6.1.30

3 entries

2.7.1.35

42 entries

2.7.1.49

3 entries

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.9

1

-

-

348531

References & Links

Literature References (125)

top print hide

Show Reference (125 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3969

5110120

_ber eine Valin-carboxylase aus Bacillus sphaericus

1971

Bast, E.; Hartmann, T.; Steiner, M.

Arch. Mikrobiol.

79

12-24

4080

-

Arginine decarboxylase of oat seedlings

1979

Smith, T.A.

Phytochemistry

18

1447-1452

4086

4870599

Arginine decarboxylase from Escherichia coli: Arginine decarboxylase from escherichia coli. I. Purification and specificity for substrates and coenzyme

1968

Blethen, S.L.; Boeker, E.A.; Snell, E.E.

J. Biol. Chem.

243

1671-1677

4407

6061681

Investigations on pantothenic acid and its related compounds

1967

Abiko, Y.

J. Biochem.

61

300-308

4409

-

Pantothenic acid and coenzyme A: phosphopantothenoylcysteine decarboxylase from rat liver [4'-phospho-N-(D-pantothenoyl)-L-cysteine carboxy-lyase, EC 4.1.1.36]

1970

Abiko, Y.

Methods Enzymol.

18

354-364

4415

3307915

Purification and properties of Escherichia coli 4'-phosphopantothenoylcysteine decarboxylase: presence of covalently bound pyruvate

1987

Yang, H.; Abeles, R.H.

Biochemistry

26

4076-4081

34693

5569129

Transsulfuration in higher plants. Partial purification and properties of beta-cystathionase of spinach

1971

Giovanelli, J.; Mudd, S.H.

Biochim. Biophys. Acta

227

654-670

37432

7417280

Inhibitors of glyoxalase enzymes

1980

Oray, B.; Norton, S.J.

Biochem. Biophys. Res. Commun.

95

624-629

80781

4306030

The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase

1969

Burg, R.W.; Snell, E.E.

J. Biol. Chem.

244

2585-2589

136067

-

Partial purification and properties of invertase from Carica papaya fruits

1988

Lopez, M.E.; Vattuone, M.A.; Sampietro, A.R.

Phytochemistry

27

3077-3081

136087

16664223

Wheat invertases. Characterization of cell wall-bound and soluble forms

1985

Krishnan, H.B.; Blanchette, J.T.; Okita, T.W.

Plant Physiol.

78

241-245

136102

3988740

Purification and characterization of Ricinus communis invertase

1985

Prado, F.E.; Vattuone, M.A.; Fleischmacher, O.L.; Sampietro, A.R.

J. Biol. Chem.

260

4952-4957

136110

-

Invertases in oat seedlings

1980

Pressey, R.; Avants, J.K.

Plant Physiol.

65

135-140

136125

8310063

Purification and characterization of three soluble invertases from barley (Hordeum vulgare L.) leaves

1993

Obenland, D.M.; Simmen, U.; Boller, T.; Wiemken, A.

Plant Physiol.

101

1331-1339

210711

5130998

Inhibition of delta-aminolaevulate dehydratase by pyridoxal derivatives and by cyanide

1971

Van Heyningen, S.; Shemin, D.

Biochem. J.

124

68P

286165

4402936

Triphosphopyridine nucleotide-linked aldehyde reductase I. Purification and properties of the enzyme from pig kidney cortex

1972

Bosron, W.F.; Prairie, R.L.

J. Biol. Chem.

217

4480-4485

287235

13715611

Purification and characterization of a TPN-dependent pyridoxol dehydrogenase from brewers yeast

1961

Holzer, H.; Schneider, S.

Biochim. Biophys. Acta

48

71-76

287236

10438489

Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase

1999

Nakano, M.; Morita, T.; Yamamoto, T.; Sano, H.; Ashiuchi, M.; Masui, R.; Kuramitsu, S.; Toshiharu, Y.

J. Biol. Chem.

274

23185-23190

287851

5769992

The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine

1969

Sundaram, T.K.; Snell, E.E.

J. Biol. Chem.

244

2577-2584

287852

3533935

Enzymes of vitamin B6 degradation. Purification and properties of pyridoxine 5-dehydrogenase (oxidase)

1986

Jong, Y.J.; Nelson, M.J.K.; Snell, E.E.

J. Biol. Chem.

261

15102-15105

348531

10672018

Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase

2000

Breton, J.; Avanzi, N.; Magagnin, S.; Covini, N.; Magistrelli, G.; Cozzi, L.; Isacchi, A.

Eur. J. Biochem.

267

1092-1099

390214

-

Control of glycolaldehyde dehydrogenase in vitamin B6 biosynthesis in Escherichia coli B

1978

Morita, H.; Tani, Y.; Ogata, K.

Agric. Biol. Chem.

42

69-73

390406

6950197

Molybdenum hydroxylases in Drosophila. II. Molybdenum cofactor in xanthine dehydrogenase, aldehyde oxidase and pyridoxal oxidase

1981

Warner, C.K.; Finnerty, V.

Mol. Gen. Genet.

184

92-96

390415

4256441

Aldehyde oxidase: catalysis of the oxidation of N 1 -methylnicotinamide and pyridoxal

1971

Stanulovic, M.; Chaykin, S.

Arch. Biochem. Biophys.

145

27-34

390445

-

Preliminary characterization and physical properties of pyridoxal oxidase from Drosophila melanogaster

1980

Hanly, E.W.

Mol. Gen. Genet.

180

455-462

390446

6808989

Tissue-specific and substrate-specific detection of aldehyde and pyridoxal oxidase in larval and imaginal tissues of Drosophila melanogaster

1982

Cypher, J.J.; Tedesco, J.L.; Courtright, J.B.; Kumaran, A.K.

Biochem. Genet.

20

315-332

390447

3136961

Minute mutations of Drosophila melanogaster change aldehyde oxidase and pyridoxal oxidase distribution patterns in imaginal wing discs

1988

Van Zijll Langhout, B.W.; Sprey, T.E.

Dev. Genet.

9

167-180

391601

4401128

Bovine liver glutamate dehydrogenase. Equilibria and kinetics of inactivation by pyridoxal

1971

Piszkiewicz, D.; Smith, E.L.

Biochemistry

10

4538-4544

391736

4084235

The inhibition of protein-lysine 6-oxidase by various lathyrogens. Evidence for two different mechanisms

1985

Levene, C.I.; Carrington, M.J.

Biochem. J.

232

293-296

391739

4838158

Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta

1974

Harris, E.D.; Gonnerman, W.A.; Savage, J.E.; O'Dell, B.L.

Biochim. Biophys. Acta

341

332-344

391740

2468539

Protein lysine 6-oxidase (lysyl oxidase) cofactor: methoxatin (PQQ) or pyridoxal?

1988

Levene, C.I.; O'Shea, M.P.; Carrington, M.J.

Int. J. Biochem.

20

1451-1456

391873

2988502

Effect of tryptophan metabolites on the activities of rat liver pyridoxal kinase and pyridoxamine 5-phosphate oxidase in vitro

1985

Takeuchi, F.; Tsubouchi, R.; Shibata, Y.

Biochem. J.

227

537-544

488269

-

Kinetic properties of two starch phosphorylases from pea seeds

1973

Matheson, N.K.; Richardson, R.H.

Phytochemistry

17

195-200

637331

795806

O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme

1976

Yamagata, S.; Takeshima, K.

J. Biochem.

80

777-785

637633

-

Studies on vitamin b6 metabolism in microorganisms. Part X. Further purification and characterization of pyridoxamine 5'-phosphate-alpha-ketoglutarate transaminase from Clostridium kainantoi

1972

Tani, Y.; Ukita, M.; Ogata, K.

Agric. Biol. Chem.

36

181-188

639956

14004227

Enzymatic transamination pf pyridoxamine. II. Crystalline pyridoxamine-pyruvate transaminase

1962

Wada, H.; Snell, E.E.

J. Biol. Chem.

237

133-137

639957

5650371

Relation of structure to activity of pyridoxal analogs as substrates for pyridoxamine pyruvate transaminase

1968

Ayling, J.E.; Snell, E.E.

Biochemistry

7

1626-1636

639958

-

Effect of pH and temperature on kinetic parameters of pyridoxamine-pyruvate transaminase

1978

Ford, J.B.

J. Ala. Acad. Sci.

49

16-30

639959

21680

Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5-deoxypyridoxal

1977

Gilmer, P.J.; McIntire, W.S.; Kirsch, J.F.

Biochemistry

16

5241-5246

639960

21681

Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5-deoxypyridoxal with the enzyme

1977

Gilmer, P.J.; Kirsch, J.F.

Biochemistry

16

5246-5253

639961

14004226

Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha-ketoglutarate

1962

Wada, H.; Snell, E.E.

J. Biol. Chem.

237

127-132

641403

13773826

Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties

1961

McCormick, D.B.; Gregory, M.E.; Snell, E.E.

J. Biol. Chem.

236

2076-2084

641404

13773827

Pyridoxal phosphokinase. II. Effects of inhibitors

1961

McCormick, D.B.; Snell, E.E.

J. Biol. Chem.

236

2085-2088

641405

8384299

Purification and properties of pyridoxal kinase from bovine brain

1993

Hirakawa-Sakurai, T.; Ohkawa, K.; Matsuda, M.

Mol. Cell. Biochem.

119

203-207

641406

3018716

Purification and characterization of pyridoxal kinase from human erythrocytes

1986

Kerry, J.A.; Kwok, F.

Prep. Biochem.

16

199-216

641407

13789

Pyridoxine kinase activity in human erythrocytes and leukocytes: assay and properties

1976

Solomon, L.R.; Hillman, R.S.

Biochem. Med.

16

223-233

641408

238769

Purification and characterization of human erythrocyte pyridoxine kinase

1975

Chern, C.J.; Beutler, E.

Clin. Chim. Acta

61

353-365

641409

4356198

Inhibition of pyridoxal kinase from rat liver in vitro by aromatic and aliphatic amines

1973

Gaeng, V.; von Collins, E.N.

Int. J. Vitam. Nutr. Res.

43

318-323

641410

2538437

Crystallization and preliminary X-ray studies of pyridoxal kinase from sheep brain

1989

Arone, A.; Rogers, P.; Scholz, G.; Kwok, F.

J. Biol. Chem.

264

4322-4323

641411

6243125

Inhibition of pyridoxal kinase by the pyridoxal-gamma-aminobutyrate imine

1980

Abercrombie, D.M.; Martin, D.L.

J. Biol. Chem.

255

79-84

641412

6260195

The kinetic mechanism of inhibition of liver pyridoxal kinase with tryptophan metabolites

1981

Karawya, E.; Mostafa, M.H.; Osman, N.

Biochim. Biophys. Acta

657

153-158

641413

3022816

Sheep brain pyridoxal kinase: fluorescence spectroscopy of the dimeric enzyme

1986

Kwok, F.; Kerry, J.A.; Churchich, J.E.

Biochim. Biophys. Acta

874

167-173

641414

4537876

The interactions between biogenic amines and pyridoxal, pyridoxal phosphate, and pyridoxal kinase

1972

Neary, J.T.; Meneely, R.L.; Grever, M.R.; Diven, W.F.

Arch. Biochem. Biophys.

151

42-47

641415

167611

Assay for human erythrocyte pyridoxine kinase

1975

Chern, C.J.; Beutler, E.

Anal. Biochem.

67

97-109

641417

3015616

Brain pyridoxal kinase. Purification and characterization

1986

Kerry, J.A.; Rohde, M.; Kwok, F.

Eur. J. Biochem.

158

581-585

641418

221500

Brain pyridoxal kinase. Purification, substrate specificities, and sensitized photodestruction of an essential histidine

1979

Kwok, F.; Churchich, J.E.

J. Biol. Chem.

254

6489-6495

641419

6285827

Physical and kinetic properties of sheep liver pyridoxine kinase

1982

Karawya, E.; Fonda, M.L.

Arch. Biochem. Biophys.

216

170-177

641420

12198308

Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain

2002

Li, M.H.; Kwok, F.; An, X.M.; Chang, W.R.; Lau, C.K.; Zhang, J.P.; Liu, S.Q.; Leung, Y.C.; Jiang, T.; Liang, D.C.

Acta Crystallogr. Sect. D

58

1479-1481

641421

10395444

Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues

1999

Maras, B.; Valiante, S.; Orru, S.; Simmaco, M.; Barra, D.; Churchich, J.E.

J. Protein Chem.

18

259-268

641422

12068103

SOS4, a pyridoxal kinase gene, is required for root hair development in Arabidopsis

2002

Shi, H.; Zhu, J.K.

Plant Physiol.

129

585-593

641423

9537380

Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12

1998

Yang, Y.; Tsui, H.C.; Man, T.K.; Winkler, M.E.

J. Bacteriol.

180

1814-1821

641424

9354586

Mechanisms of the inhibition of human erythrocyte pyridoxal kinase by drugs

1997

Laine-Cessac, P.; Cailleux, A.; Allain, P.

Biochem. Pharmacol.

54

863-870

641425

10987144

Human pyridoxal kinase: overexpression and properties of the recombinant enzyme

2000

Lee, H.S.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.

Mol. Cells

10

452-459

641426

9274862

Characterization of Trypanosoma brucei pyridoxal kinase: purification, gene isolation and expression in Escherichia coli

1997

Scott, T.C.; Phillips, M.A.

Mol. Biochem. Parasitol.

88

1-11

641427

-

Catalytic and structural properties of pyridoxal kinase

1997

Cho, J.J.; Kim, S.K.; Kim, Y.T.

J. Biochem. Mol. Biol.

30

125-131

641428

9252787

Kinetic studies of the effects of K+, Na+, and Li+ on the catalytic activity of human erythrocyte pyridoxal kinase

1997

Laine-Cessac, P.; Allain, P.

Enzyme Protein

49

291-304

641429

11983425

Study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor

2002

Fong, C.C.; Lai, W.P.; Leung, Y.C.; Lo, S.C.; Wong, M.S.; Yang, M.

Biochim. Biophys. Acta

1596

95-107

641658

2540841

Purification and properties of hydroxymethylpyrimidine kinase from Escherichia coli

1989

Mizote, T.; Nakayama, H.

Biochim. Biophys. Acta

991

109-113

644595

4293967

Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster: II. Enzyme kinetics

1967

Yen, T.T.T.; Glassman, E.

Biochim. Biophys. Acta

146

35-44

651405

11024303

Purple acid phosphatases from bacteria: similarities to mammalian and plant enzymes

2000

Schenk, G.; Korsinczky, M.L.J.; Hume, D.A.; Hamilton, S.; DeJersey, J.

Gene

255

419-424

651458

11857742

Structure, genomic DNA typing, and kinetic characterization of the D allozyme of placental alkaline phosphatase (PLAP/ALPP)

2002

Wennberg, C.; Kozlenkov, A.; Di Mauro, S.; Frohlander, N.; Beckman, L.; Hoylaerts, M.F.; Millan, J.L.

Hum. Mutat.

19

258-267

651551

10794613

Biochemical characterization of cystine lyase from broccoli (Brassica oleracea var. italica)

1999

Ramirez, E.C.; Whitaker, J.R.

J. Agric. Food Chem.

47

2218-2225

651559

12405788

Purification and characterization of three phytases from germinated lupine seeds (Lupinus albus var. amiga)

2002

Greiner, R.

J. Agric. Food Chem.

50

6858-6864

655029

12005047

Purification and characterization of pyridoxal 4-dehydrogenase from Aureobacterium luteolum

2002

Trongpanich, Y.; Abe, K.; Kaneda, Y.; Morita, T.; Yagi, T.

Biosci. Biotechnol. Biochem.

66

543-548

655965

1322411

Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes

1992

Fonda, M.L.

J. Biol. Chem.

267

15978-15983

656239

15226311

Molecular cloning, expression, and properties of an unusual aldo-keto reductase family enzyme, pyridoxal 4-dehydrogenase, that catalyzes irreversible oxidation of pyridoxal

2004

Yokochi, N.; Yoshikane, Y.; Trongpanich, Y.; Ohnishi, K.; Yagi, T.

J. Biol. Chem.

279

37377-37384

662007

14973012

Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase

2004

Park, J.H.; Burns, K.; Kinsland, C.; Begley, T.P.

J. Bacteriol.

186

1571-1573

662055

14688239

Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes

2003

Cheung, P.Y.; Fong, C.C.; Ng, K.T.; Lam, W.C.; Leung, Y.C.; Tsang, C.W.; Yang, M.; Wong, M.S.

J. Biochem.

134

731-738

662200

14722069

Conformational changes in the reaction of pyridoxal kinase

2004

Li, M.H.; Kwok, F.; Chang, W.R.; Liu, S.Q.; Lo, S.C.; Zhang, J.P.; Jiang, T.; Liang, D.C.

J. Biol. Chem.

279

17459-17465

662402

15985434

Crystal structure of pyridoxal kinase in complex with roscovitine and derivatives

2005

Tang, L.; Li, M.H.; Cao, P.; Wang, F.; Chang, W.R.; Bach, S.; Reinhardt, J.; Ferandin, Y.; Galons, H.; Wan, Y.; Gray, N.; Meijer, L.; Jiang, T.; Liang, D.C.

J. Biol. Chem.

280

31220-31229

662440

15590634

Analysis of the vitamin B6 biosynthesis pathway in the human malaria parasite Plasmodium falciparum

2005

Wrenger, C.; Eschbach, M.L.; Muller, I.B.; Warnecke, D.; Walter, R.D.

J. Biol. Chem.

280

5242-5248

662961

15381280

Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia

2004

Hwang, I.K.; Yoo, K.Y.; Kim, D.S.; Eum, W.S.; Park, J.K.; Park, J.; Kwon, O.S.; Kang, T.C.; Choi, S.Y.; Won, M.H.

Neuroscience

128

511-518

663303

15249053

Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases

2004

di Salvo, M.L.; Hunt, S.; Schirch, V.

Protein Expr. Purif.

36

300-306

667329

16824480

Identification of a new tetrameric pyridoxal 4-dehydrogenase as the second enzyme in the degradation pathway for pyridoxine in a nitrogen-fixing symbiotic bacterium, Mesorhizobium loti

2006

Yokochi, N.; Nishimura, S.; Yoshikane, Y.; Ohnishi, K.; Yagi, T.

Arch. Biochem. Biophys.

452

1-8

671140

17012797

Cloning, purification and preliminary crystallographic analysis of a putative pyridoxal kinase from Bacillus subtilis

2006

Newman, J.A.; Das, S.K.; Sedelnikova, S.E.; Rice, D.W.

Acta Crystallogr. Sect. F

F62

1006-1009

671864

16545075

Molecular cloning, expression and characterization of pyridoxamine-pyruvate aminotransferase

2006

Yoshikane, Y.; Yokochi, N.; Ohnishi, K.; Hayashi, H.; Yagi, T.

Biochem. J.

396

499-507

672438

15820755

Tat-mediated protein transduction of human brain pyridoxal kinase into PC12 cells

2005

Kim, D.W.; Kim, C.K.; Choi, S.H.; Choi, H.S.; Kim, S.Y.; An, J.J.; Lee, S.R.; Lee, S.H.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, Y.J.; Cho, S.W.; Kang, J.H.; Kim, T.Y.; Lee, K.S.; Park, J.; Eum, W.S.; Choi, S.Y.

Biochimie

87

481-487

673580

17250738

The human pyridoxal kinase, a plausible target for ginkgotoxin from Ginkgo biloba

2007

Kaestner, U.; Hallmen, C.; Wiese, M.; Leistner, E.; Drewke, C.

FEBS J.

274

1036-1045

675407

16978644

The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution

2006

Newman, J.A.; Das, S.K.; Sedelnikova, S.E.; Rice, D.W.

J. Mol. Biol.

363

520-530

675693

16600635

Crystal structure of human pyridoxal kinase

2006

Cao, P.; Gong, Y.; Tang, L.; Leung, Y.C.; Jiang, T.

J. Struct. Biol.

154

327-332

677029

17766369

Crystal Structure of human pyridoxal kinase: Structural basis of M+ and M2+ activation

2007

Musayev, F.N.; Di Salvo, M.L.; Ko, T.P.; Gandhi, A.K.; Goswami, A.; Schirch, V.; Safo, M.K.

Protein Sci.

16

2184-2194

678498

17116355

Molecular modelling studies on the interactions of human DNA topoisomerase IB with pyridoxal-compounds

2007

Christmann-Franck, S.; Fermandjian, S.; Mirambeau, G.; Der Garabedian, P.A.

Biochimie

89

468-473

688568

18388403

Determination of individual vitamin B(6) compounds based on enzymatic conversion to 4-pyridoxolactone

2008

Nishimura, S.; Nagano, S.; A Crai, C.; Yokochi, N.; Yoshikane, Y.; Ge, F.; Yagi, T.

J. Nutr. Sci. Vitaminol.

54

18-24

691701

18066686

Mammalian aldehyde oxidases: genetics, evolution and biochemistry

2008

Garattini, E.; Fratelli, M.; Terao, M.

Cell. Mol. Life Sci.

65

1019-1048

699047

19111641

Synthesis of 4-pyridoxolactone from pyridoxine using a combination of transformed Escherichia coli cells

2008

Tamura, A.; Yoshikane, Y.; Yokochi, N.; Yagi, T.

J. Biosci. Bioeng.

106

460-465

702038

19351586

Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase

2009

Gandhi, A.K.; Ghatge, M.S.; Musayev, F.N.; Sease, A.; Aboagye, S.O.; di Salvo, M.L.; Schirch, V.; Safo, M.K.

Biochem. Biophys. Res. Commun.

381

12-15

702184

4407783

Ornithine degradation in Clostridium sticklandii: pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl-CoA

1974

Jeng, I.M.; Somack, R.; Barker, H.A.

Biochemistry

13

2989-2903

706419

19197387

Poisoning pyridoxal 5-phosphate-dependent enzymes: a new strategy to target the malaria parasite Plasmodium falciparum

2009

Mueller, I.B.; Wu, F.; Bergmann, B.; Knoeckel, J.; Walter, R.D.; Gehring, H.; Wrenger, C.

PLoS ONE

4

e4406

710764

20516609

Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti

2010

Chu, H.N.; Kobayashi, J.; Yoshikane, Y.; Mikami, B.; Yagi, T.

Acta Crystallogr. Sect. F

66

718-720

721873

21307574

The crystal structure of SDR-type pyridoxal 4-dehydrogenase of Mesorhizobium loti

2011

Chu, H.N.; Kobayashi, J.; Mikami, B.; Yagi, T.

Biosci. Biotechnol. Biochem.

75

388-390

722183

-

Recombinant expression, purification and characterization of Bombyx mori (Lepidoptera: Bombycidae) pyridoxal kinase

2011

Huang, S.; Ma, W.; Zhang, P.; Zhang, J.; Xie, Y.; Huang, L.

Eur. J. Entomol.

108

25-34

723219

22857512

Chemical, genetic and structural assessment of pyridoxal kinase as a drug target in the African trypanosome

2012

Jones, D.C.; Alphey, M.S.; Wyllie, S.; Fairlamb, A.H.

Mol. Microbiol.

86

51-64

723449

23321022

The SOS4 pyridoxal kinase is required for maintenance of vitamin B6-mediated processes in chloroplasts

2013

Rueschhoff, E.E.; Gillikin, J.W.; Sederoff, H.W.; Daub, M.E.

Plant Physiol. Biochem.

63

281-291

723578

22879864

Crystal structures of human pyridoxal kinase in complex with the neurotoxins, ginkgotoxin and theophylline: insights into pyridoxal kinase inhibition

2012

Gandhi, A.K.; Desai, J.V.; Ghatge, M.S.; di Salvo, M.L.; Di Biase, S.; Danso-Danquah, R.; Musayev, F.N.; Contestabile, R.; Schirch, V.; Safo, M.K.

PLoS ONE

7

e40954

730629

22698754

Characterization of an acid phosphatase responsible for hydrolysis of pyridoxal 5-phosphate in tobacco plants

2012

Huang, S.; Zhang, J.; Ma, Y.; Wei, S.; Huang, L.

Plant Physiol. Biochem.

57

114-119

737378

25372829

Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK)

2014

Kronenberger, T.; Lunev, S.; Wrenger, C.; Groves, M.R.

Acta Crystallogr. Sect. F

70

1550-1555

737622

27425248

Crystal structure and catalytic mechanism of pyridoxal kinase from Pseudomonas aeruginosa

2016

Kim, M.I.; Hong, M.

Biochem. Biophys. Res. Commun.

478

300-306

737767

25655354

On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5-phosphate

2015

di Salvo, M.L.; Nogues, I.; Parroni, A.; Tramonti, A.; Milano, T.; Pascarella, S.; Contestabile, R.

Biochim. Biophys. Acta

1854

1160-1166

737809

23860900

Catalytic and regulatory roles of species involved in metal-nucleotide equilibriums in human pyridoxal kinase

2013

Navarro, F.; Ramirez-Sarmiento, C.A.; Guixe, V.

Biometals

26

805-812

738236

25157434

The antimalarial drugs chloroquine and primaquine inhibit pyridoxal kinase, an essential enzyme for vitamin B6 production

2014

Kimura, T.; Shirakawa, R.; Yaoita, N.; Hayashi, T.; Nagano, K.; Horiuchi, H.

FEBS Lett.

588

3673-3676

738451

24601602

A subfamily of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage

2014

Nodwell, M.B.; Koch, M.F.; Alte, F.; Schneider, S.; Sieber, S.A.

J. Am. Chem. Soc.

136

4992-4999

739366

-

Enzymatic transamination of pyridoxamine in tobacco plants

2013

Huang, S.; Zhang, J.; Wu, M.; Wu, Q.; Huang, L.

Plant Sci.

212

55-59

740812

24737760

The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificities

2014

Marelja, Z.; Dambowsky, M.; Bolis, M.; Georgiou, M.L.; Garattini, E.; Missirlis, F.; Leimkuehler, S.

J. Exp. Biol.

217

2201-2211

758844

30928491

Discovery of pyridoxal reductase activity as part of human vitamin B6 metabolism

2019

Ramos, R.J.; Albersen, M.; Vringer, E.; Bosma, M.; Zwakenberg, S.; Zwartkruis, F.; Jans, J.J.M.; Verhoeven-Duif, N.M.

Biochim. Biophys. Acta

1863

1088-1097

758844

30928491

Discovery of pyridoxal reductase activity as part of human vitamin B6 metabolism

2019

Ramos, R.J.; Albersen, M.; Vringer, E.; Bosma, M.; Zwakenberg, S.; Zwartkruis, F.; Jans, J.J.M.; Verhoeven-Duif, N.M.

Biochim. Biophys. Acta

1863

1088-1097

758844

2 entries

759093

-

The crystal structure of the Plasmodium falciparum PdxK provides an experimental model for pro-drug activation

2019

Gao, K.; Wang, W.; Kronenberger, T.; Wrenger, C.; Groves, M.

Crystals

9

534

759126

28648182

Biotransformation of pyridoxal 5-phosphate from pyridoxal by pyridoxal kinase (pdxY) to support cadaverine production in Escherichia coli

2017

Kim, J.H.; Kim, J.; Kim, H.J.; Sathiyanarayanan, G.; Bhatia, S.K.; Song, H.S.; Choi, Y.K.; Kim, Y.G.; Park, K.; Yang, Y.H.

Enzyme Microb. Technol.

104

9-15

759126

28648182

Biotransformation of pyridoxal 5-phosphate from pyridoxal by pyridoxal kinase (pdxY) to support cadaverine production in Escherichia coli

2017

Kim, J.H.; Kim, J.; Kim, H.J.; Sathiyanarayanan, G.; Bhatia, S.K.; Song, H.S.; Choi, Y.K.; Kim, Y.G.; Park, K.; Yang, Y.H.

Enzyme Microb. Technol.

104

9-15

759126

2 entries

759183

31116912

Structural and functional studies on Salmonella typhimurium pyridoxal kinase the first structural evidence for the formation of Schiff base with the substrate

2019

Deka, G.; Kalyani, J.N.; Jahangir, F.B.; Sabharwal, P.; Savithri, H.S.; Murthy, M.R.N.

FEBS J.

286

3684-3700

759342

30031075

Pyridoxal kinase a vitamin B6 salvage pathway enzyme from Leishmania donovani

2018

Kumar, V.; Sharma, M.; Rakesh, B.R.; Malik, C.K.; Neelagiri, S.; Neerupudi, K.B.; Garg, P.; Singh, S.

Int. J. Biol. Macromol.

119

320-334

759342

30031075

Pyridoxal kinase a vitamin B6 salvage pathway enzyme from Leishmania donovani

2018

Kumar, V.; Sharma, M.; Rakesh, B.R.; Malik, C.K.; Neelagiri, S.; Neerupudi, K.B.; Garg, P.; Singh, S.

Int. J. Biol. Macromol.

119

320-334

759346

32105687

Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani

2020

Are, S.; Gatreddi, S.; Jakkula, P.; Qureshi, I.A.

Int. J. Biol. Macromol.

152

812-827

759346

32105687

Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani

2020

Are, S.; Gatreddi, S.; Jakkula, P.; Qureshi, I.A.

Int. J. Biol. Macromol.

152

812-827

760178

31578392

The expression of four pyridoxal kinase (PDXK) human variants in Drosophila impacts on genome integrity

2019

Mascolo, E.; Barile, A.; Mecarelli, L.S.; Amoroso, N.; Merigliano, C.; Massimi, A.; Saggio, I.; Hansen, T.; Tramonti, A.; Di Salvo, M.L.; Barbetti, F.; Contestabile, R.; Verni, F.

Sci. Rep.

9

14188

760178

31578392

The expression of four pyridoxal kinase (PDXK) human variants in Drosophila impacts on genome integrity

2019

Mascolo, E.; Barile, A.; Mecarelli, L.S.; Amoroso, N.; Merigliano, C.; Massimi, A.; Saggio, I.; Hansen, T.; Tramonti, A.; Di Salvo, M.L.; Barbetti, F.; Contestabile, R.; Verni, F.

Sci. Rep.

9

14188

759342

2 entries

759346

2 entries

760178

2 entries

Links to other databases for pyridoxal

top print hide

Show Links (1 entry)