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Ligand decanal

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.3

decanal + FMNH + O2 = decanoic acid + FMN + H2O + light

348578, 348550, 348560, 348580, 348582, 348585, 348587, 348596, 348556, 348586, 348590, 348591, 348593, 348561, 348545, 348546, 348547, 348548, 348549, 348551, 348552, 348553, 348554, 348555, 348557, 348558, 348559, 348562, 348564, 348565, 348566, 348567, 348568, 348569, 348570, 348571, 348572, 348573, 348574, 348575, 348576, 348577, 348579, 348581, 348583, 348584, 348588, 348589, 348597, 348599, 348600, 348601, 348543, 348598, 348544, 348563, 348542, 348592, 348594, 348595

-

1.14.14.3

n-caprinaldehyde + FMNH2 + O2 = n-caprinoate + FMN + H2O + hv

676010

-

1.2.1.16

decanal + NAD+ + H2O = decanoate + NADH + H+

726463

-

1.2.1.16

decanal + NADP+ + H2O = decanoate + NADPH + H+

726463

-

1.14.14.3

2 entries

1.2.1.16

2 entries

Substrate in Enzyme-catalyzed Reactions (47 results)

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Show Substrate (47 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

decyl aldehyde + NADH + H+ = 1-decanol + NAD+

678779

-

1.1.1.145

caprinaldehyde + NADPH = ?

389394

-

1.1.1.184

decanal + NADPH = decanol + NADP+

347755

-

1.1.1.192

decanal + NAD+ + H+ = decanoic acid + NADH

712962

-

1.1.1.2

decanal + NADPH + H+ = decanol + NADP+

698623

-

1.1.1.2

decanal + NADPH = decanol + NADP+

695771

-

1.1.1.2

n-decanal + NADPH + H+ = n-decanol + NADP+

286183, 286210, 286205

-

1.1.1.21

1-decanal + NADPH + H+ = 1-decanol + NADP+

697266

-

1.1.1.21

decanal + NAD(P)H = decanol + NAD(P)+

286240

-

1.1.1.2

3 entries

1.1.1.21

2 entries

1.1.1.71

decanal + NAD(P)H = decan-1-ol + NAD(P)+

287282

-

1.1.1.90

decanal + NADH + H+ = decanol + NAD+

724027

-

1.1.1.91

decanal + NADPH = decanol + NADP+

724669

-

1.14.14.3

decanal + FMNH + O2 = decanoic acid + FMN + H2O + light

348578, 348550, 348560, 348580, 348582, 348585, 348587, 348596, 348556, 348586, 348590, 348591, 348593, 348561, 698992, 704579, 348545, 348546, 348547, 348548, 348549, 348551, 348552, 348553, 348554, 348555, 348557, 348558, 348559, 348562, 348564, 348565, 348566, 348567, 348568, 348569, 348570, 348571, 348572, 348573, 348574, 348575, 348576, 348577, 348579, 348581, 348583, 348584, 348588, 348589, 348597, 348599, 348600, 348601, 348602, 348604, 348607, 348608, 348543, 348598, 348544, 348563, 348542, 348592, 348594, 348595, 702318

-

1.14.14.3

decanal + FMNH- + O2 = decanoic acid + FMN + H2O + hv

727031

-

1.14.14.3

decanal + FMNH2 + O2 = decanoate + FMN + H2O + hn

744492, 657939, 658050, 658060, 657923

-

1.14.14.3

decanal + FMNH2 + O2 = decanoate + FMN + H2O + hnu

744675

-

1.14.14.3

decanal + FMNH2 + O2 = decanoate + FMN + H2O + hv

671610, 671978, 671985

-

1.14.14.3

decanal + FMNH2 + O2 = decanoic acid + FMN + H2O + hnu

728228

-

1.14.14.3

decanal + FMNH2 + O2 = decanoic acid + FMN + H2O + hv

726764, 728435, 728284

-

1.14.14.3

decanal + riboflavin + O2 = ?

698992

-

1.14.14.3

n-caprinaldehyde + FMNH2 + O2 = n-caprinoate + FMN + H2O + hv

676010

-

1.14.14.3

n-decanal + FMNH2 + O2 = n-decanoate + FMN + H2O + hn

658147

-

1.2.1.16

decanal + NAD+ + H2O = decanoate + NADH + H+

726463

-

1.2.1.16

decanal + NADP+ + H2O = decanoate + NADPH + H+

726463

-

1.2.1.3

decanal + NAD+ + H2O = decanaote + NADH

655643

-

1.2.1.3

decanal + NAD+ + H2O = decanoate + NADH

348694, 348691, 348716, 348704, 348699, 348681, 348725, 348706, 348722

-

1.2.1.3

decanaldehyde + NAD+ + H2O = decanoate + NADH + H+

712957

-

1.2.1.36

decanal + NAD+ + H2O = decanoate + NADH

656252

-

1.2.1.36

decanal + NAD+ + H2O = decanoate + NADH + 2 H+

742258

-

1.2.1.36

decanal + NAD+ + H2O = decanoate + NADH + H+

724722, 671851

-

1.2.1.36

decanal + NAD+ + H2O = decanoic acid + NADH

390270, 390274

-

1.14.14.3

10 entries

1.2.1.16

2 entries

1.2.1.3

3 entries

1.2.1.36

4 entries

1.2.1.39

decanal + NAD+ + H2O = decanoate + NADH + H+

690567

-

1.2.1.4

decanal + NADP+ = decanoate + NADPH

348725, 437830, 437831

-

1.2.1.48

decanal + NAD+ + H2O = decanoic acid + NADH

390324, 390320, 94404, 389732

-

1.2.1.48

decanal + NAD+ + H2O = decanoic acid + NADH + H+

693389

-

1.2.1.48

2 entries

1.2.1.5

n-decanal + NADP+ + H2O = n-decanoate + NADPH + H+

671511

-

1.2.1.94

decanal + NAD+ + H2O = decanoic acid + NADH + 2 H+

742654

-

1.2.1.94

decanal + NAD+ + H2O = decanoic acid + NADH + H+

725133

-

1.2.1.94

2 entries

1.2.3.1

decylaldehyde + H2O + O2 = decanoate + H2O2

656311

-

1.2.5.2

decanal + a quinone + H2O = decanoate + a quinol

288472

-

1.2.99.6

decylaldehyde + 2,6-dichlorophenol indophenol = decanoate + reduced 2,6-dichlorophenol indophenol

654439

-

4.1.2.10

cyanide + decanal = (2R)-2-hydroxyundecanal

701695

-

4.1.2.10

HCN + decanal = (R)-2-hydroxyundecanenitrile

663419

-

4.1.2.47

cyanide + decanal = (2S)-2-hydroxyundecanenitrile

650854

-

4.1.2.47

HCN + decanal = (S)-2-hydroxyundecanenitrile

663419

-

4.1.99.5

decanal + O2 + 2 NADH + 2 H+ = nonane + formate + H2O + 2 NAD+

726548

-

4.1.99.5

n-decanal + O2 + 2 NADPH + 2 H+ = n-nonane + formate + H2O + 2 NADP+

748027, 747351

-

4.1.2.10

2 entries

4.1.2.47

2 entries

4.1.99.5

2 entries

Product in Enzyme-catalyzed Reactions (21 results)

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Show Product (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

1-decanol + NAD+ = decanal + NADH + H+

-

-

1.1.1.1

n-decanol + NAD+ = n-decanal + NADH

-

-

1.1.1.1

2 entries

1.1.1.192

n-decanol + NAD+ + H2O = n-decanal + NADH

-

-

1.1.1.2

decanol + NADP+ = decanal + NADPH + H+

-

-

1.1.1.21

1-decanol + NADP+ = decanal + NADPH + H+

-

-

1.1.1.216

decanol + NADP+ = decanal + NADPH

-

-

1.1.1.71

decan-1-ol + NADP+ = decanal + NADPH

287277

-

1.1.3.13

1-decanol + O2 = decanal + H2O2

-

-

1.1.3.13

decanol + O2 = decanal + H2O2

-

-

1.1.3.13

lactate + O2 = decanal + H2O2

-

-

1.1.3.13

3 entries

1.1.3.18

1-decanol + O2 = n-decanal + H2O2

-

-

1.1.3.20

decanol + O2 = decanal + H2O2

, 389732

-

1.1.99.20

1-decanol + acceptor = n-decanal + reduced acceptor

389904

-

1.14.11.77

decyl sulfate + 2-oxoglutarate + O2 = decanal + succinate + CO2 + sulfate

-

-

1.14.14.5

decanesulfonic acid + FMNH2 + O2 = decanal + FMN + sulfite + H2O

-

-

1.2.1.30

capric acid + ATP + NADPH + H+ = capraldehyde + AMP + diphosphate + NADP+

-

-

1.2.1.42

decanoyl-CoA + NAD(P)H = decanal + NAD(P)+

288215

-

1.3.1.27

trans-2-decenal + NAD(P)H = decanal + NAD(P)+

390629, 390627

-

1.3.1.31

(E)-2-decenal + NADH + H+ = decanal + NAD+

-

-

1.3.1.48

trans-2-decenal + NADPH + H+ = decanal + NADP+

-

-

1.3.1.48

trans-2-decenal + NADPH = decanal + NADP+

390830

-

1.3.1.48

2 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.3

-

348601

-

1.14.14.3

reversible substrate inhibition, depending on phosphate concentration

348571

-

1.14.14.3

2 entries

1.2.1.4

substrate inhibition

437830

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

1.2.1.71

5u0l, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.21

0.35

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.2.1.3

3.83

-

enzyme form ALDH-1, pH 9.5

348694

1.2.1.3

11.7

-

enzyme form ALDH-2, pH 9.5

348694

1.2.1.36

0.4

-

wild-type

671851

1.2.1.36

1

-

pH 8.5, 25°C, recombinant enzyme

742258

1.2.1.36

2.2

-

pH 8.5, 25°C, recombinant enzyme

742258

1.2.1.36

2.2

-

wild type enzyme ALDH1A2, at pH 8.5 and 25°C

724722

1.2.1.3

2 entries

1.2.1.36

4 entries

1.2.1.48

2.18

-

-

693389

1.2.99.6

1.19

-

25°C, pH 8.0, enzyme in aqueous solution

654439

1.2.99.6

1.22

-

25°C, pH 8.0, enzyme in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles, hydratation degree 26

654439

1.2.99.6

2 entries

K_M Value (66 results)

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Show KM Value (66 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.145

0.69

-

-

389394

1.1.1.192

0.095

-

-

347799

1.1.1.2

0.0033

-

-

286205

1.1.1.2

0.07

-

-

286183

1.1.1.2

2 entries

1.1.1.21

0.0055

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.14.14.3

0.0003

-

wild type, 50 mM phosphate

348607

1.14.14.3

0.0004

-

recombinant mutant alphaF261S, pH 7.0, 25°C

657923

1.14.14.3

0.0004

-

recombinant mutant alphaG275I, pH 7.0, 25°C

657923

1.14.14.3

0.001

-

recombinant wild-type enzyme, pH 7.0, 25°C

657923

1.14.14.3

0.00101

-

pH 7.0, 23°C, recombinant mutant F49Y

671978

1.14.14.3

0.00113

-

recombinant wild type enzyme, at 22°C, pH not specified in the publication

728435

1.14.14.3

0.0012

0.009

depending on buffer system

348571

1.14.14.3

0.0013

-

pH 7.0, 23°C, recombinant mutant F46A

671978

1.14.14.3

0.0016

-

pH 7.0, 23°C, recombinant wild-type enzyme

671978

1.14.14.3

0.0016

-

pH 7.0, 23°C, recombinant wild-type enzyme and mutant A74G

671985

1.14.14.3

0.0016

-

recombinant mutant alphaF261Y, pH 7.0, 25°C

657923

1.14.14.3

0.00165

-

luciferase-mOrange fusion enzyme, at 22°C, pH not specified in the publication

728435

1.14.14.3

0.0017

-

recombinant mutant alphaF261A, pH 7.0, 25°C

657923

1.14.14.3

0.0018

-

recombinant mutant alphaG275P, pH 7.0, 25°C

657923

1.14.14.3

0.0021

-

alphaR107S, 50 mM phosphate

348607

1.14.14.3

0.0022

-

alphaR107E, 50 mM phosphate

348607

1.14.14.3

0.0022

-

recombinant mutant alphaG275A, pH 7.0, 25°C

657923

1.14.14.3

0.0023

-

pH 7.0, 23°C, recombinant mutant E328Q

671985

1.14.14.3

0.0024

-

pH 7.0, 23°C, recombinant mutant F117S

671978

1.14.14.3

0.0024

-

pH 7.0, 23°C, recombinant mutant F46Y

671978

1.14.14.3

0.0026

-

pH 7.0, 23°C, recombinant mutant F46S

671978

1.14.14.3

0.0027

-

pH 7.0, 23°C, recombinant mutant F114Y

671978

1.14.14.3

0.0027

-

recombinant mutant alphaG275F, pH 7.0, 25°C

657923

1.14.14.3

0.003

-

pH 7.0, 23°C, recombinant mutants F49D, F117A, and F49A

671978

1.14.14.3

0.0031

-

alphaR107A, 50 mM phosphate

348607

1.14.14.3

0.0031

-

pH 7.0, 23°C, recombinant mutant F117D

671978

1.14.14.3

0.0032

-

pH 7.0, 23°C, recombinant mutant F46D

671978

1.14.14.3

0.0033

-

pH 7.0, 23°C, recombinant mutant E328A

671985

1.14.14.3

0.0033

-

pH 7.0, 23°C, recombinant mutant F49S

671978

1.14.14.3

0.0037

-

recombinant mutant alphaG284P, pH 7.0, 25°C

657923

1.14.14.3

0.0045

-

pH 7.0, 23°C, recombinant mutant E328F

671985

1.14.14.3

0.0046

-

recombinant mutant alphaF261D, pH 7.0, 25°C

657923

1.14.14.3

0.005

-

pH 7.0, 23°C, recombinant mutant E328D

671985

1.14.14.3

0.0051

-

pH 7.0, 23°C, recombinant mutant F117Y

671978

1.14.14.3

0.0073

-

pH 7.0, 23°C, recombinant mutant F114D

671978

1.14.14.3

0.008

-

wild-type

704579

1.14.14.3

0.0083

-

pH 7.0, 23°C, recombinant mutant F114S

671978

1.14.14.3

0.0093

-

pH 7.0, 23°C, recombinant mutant F114A

671978

1.14.14.3

0.0095

-

pH 7.0, 23°C, recombinant mutant E328H

671985

1.14.14.3

0.0097

-

pH 7.0, 23°C, recombinant mutant E328L

671985

1.14.14.3

0.01

-

mutant K286A

704579

1.14.14.3

0.0105

-

mutant K283A

704579

1.14.14.3

0.0173

-

pH 7.0, 23°C, recombinant mutant A74F

671985

1.14.14.3

0.11

-

pH 7.0, temperature not specified in the publication

744675

1.2.1.3

0.0000029

-

enzyme form ALDH-1, pH 9.5

348694

1.2.1.3

0.000022

-

enzyme form ALDH-2, pH 9.5

348694

1.2.1.3

0.0013

-

-

348681

1.2.1.3

0.0071

-

-

348691

1.2.1.3

91

-

+/- 20

655643

1.2.1.36

0.0003

-

-

390270

1.2.1.36

0.001

-

recombinant wild-type enzyme and mutant L459F/N460G, pH 8.5, 25°C

656252

1.2.1.36

0.0064

-

pH 8.5, 25°C, recombinant enzyme

742258

1.2.1.36

0.0064

-

wild type enzyme ALDH1A2, at pH 8.5 and 25°C

724722

1.2.1.36

0.0065

-

wild-type

671851

1.2.1.36

0.01

-

pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme

742258

1.2.1.36

0.01

-

wild type enzyme ALDH1A1, at pH 8.5 and 25°C

724722

1.2.1.4

0.0015

-

-

437830

1.2.1.4

0.023

-

-

348725

1.2.1.48

0.0038

-

-

693389

1.2.1.48

0.004

-

-

94404, 389732

1.2.1.48

0.023

-

-

390324

1.14.14.3

44 entries

1.2.1.3

5 entries

1.2.1.36

7 entries

1.2.1.4

2 entries

1.2.1.48

3 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.4

0.035

-

-

437830

References & Links

Literature References (142)

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Show Reference (142 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

94404

-

Enzymes of wax ester catabolism in jojoba

1981

Moreau, R.A.; Huang, A.H.C.

Methods Enzymol.

71

804-813

286183

6416297

Purification and properties of an NADPH-linked aldehyde reductase from rat kidney

1983

Takahashi, N.; Saito, T.; Tomita, K.

Biochim. Biophys. Acta

748

444-452

286205

9952458

Purification and characterization of a NADPH-dependent aldehyde reductase from mung bean that detoxifies eutypine, a toxin from Eutypa lata1

1999

Colrat, S.; Latche, A.; Guis, M.; Pech, J.C.; Bouzayen, M.; Fallot, J.; Roustan, J.P.

Plant Physiol.

119

621-626

286210

11097895

Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli

2000

Tani, A.; Sakai, Y.; Ishige, T.; Kato, N.

Appl. Environ. Microbiol.

66

5231-5235

286240

6815419

Aldose reductase from human tissues

1982

Wermuth, B.; von Wartburg, J.P.

Methods Enzymol.

89

181-186

287277

8162187

NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae

1994

Wales, M.R.; Fewson, C.A.

Microbiology

140

173-183

287282

4300551

The enzymatic reduction of retinal to retinol in rat intestine

1968

Fidge, N.H.; Goodman, D.S.

J. Biol. Chem.

243

4372-4379

288215

11872467

Wax ester production from n-alkanes by Acinetobacter sp. strain M-1: ultrastructure of cellular inclusions and role of acyl coenzyme A reductase

2002

Ishige, T.; Tani, a.; Takabe, K.; Kawasaki, K.; Sakai, Y.; Kato, N.

Appl. Environ. Microbiol.

68

1192-1195

288472

-

A pyridine nucleotide-independent aldehyde dehydrogenase involved in the alkane oxidation of Acetobacter rancens

1984

Hommel, R.; Kleber, H.P.

FEMS Microbiol. Lett.

22

139-142

347755

1731616

Purification and characterization of pig lung carbonyl reductase

1992

Oritani, H.; Deyashiki, Y.; Nakayama, T.; Hara, A.; Sawada, H.; Matsuura, K.; Bunai, Y.; Ohya, I.

Arch. Biochem. Biophys.

292

539-547

347799

-

Long-chain n-alkanol dehydrogenase from Pseudomonas putida

1996

Nagashima, H.; Inoue, J.; Sasaki, E.; Yamamoto, S.; Sasaki, Y.; Yamauchi-Inomata, Y.; Harayama, S.

J. Ferment. Bioeng.

82

328-333

348542

1854193

Detection of luciferase gene sequence in nonluminescent Vibrio cholerae by colony hybridization and polymerase chain reaction

1991

Palmer, L.M.; Colwell, R.R.

Appl. Environ. Microbiol.

57

1286-1293

348543

1995589

Cloning and nucleotide sequences of lux genes and characterization of luciferase of Xenorhabdus luminescens from a human wound

1991

Xi, L.; Cho, K.W.; Tu, S.C.

J. Bacteriol.

173

1399-1405

348544

2256783

Relationship of the luminous bacterial symbiont of the Caribbean flashlight fish, Kryptophanaron alfredi (family Anomalopidae) to other luminous bacteria based on bacterial luciferase (luxA) genes

1990

Haygood, M.G.

Arch. Microbiol.

154

496-503

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Crystal structure of the bacterial luciferase/flavin complex provides insight into the function of the beta subunit

2009

Campbell, Z.T.; Weichsel, A.; Montfort, W.R.; Baldwin, T.O.

Biochemistry

48

6085-6094

704579

19710008

Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates

2009

Campbell, Z.T.; Baldwin, T.O.

J. Biol. Chem.

284

32827-32834

712957

20171064

Characterization of a broad-range aldehyde dehydrogenase involved in alkane degradation in Geobacillus thermodenitrificans NG80-2

2010

Li, X.; Li, Y.; Wei, D.; Li, P.; Wang, L.; Feng, L.

Microbiol. Res.

165

706-712

712962

19383697

Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2

2009

Liu, X.; Dong, Y.; Zhang, J.; Zhang, A.; Wang, L.; Feng, L.

Microbiology

155

2078-2085

724027

23042182

Purification and characterization of an NAD+-dependent XylB-like aryl alcohol dehydrogenase identified in Acinetobacter baylyi ADP1

2012

Uthoff, S.; Steinbuechel, A.

Appl. Environ. Microbiol.

78

8743-8752

724669

22742413

Cloning, expression and characterization of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium strain BKM-F-1767

2012

Yang, D.D.; Francois, J.M.; de Billerbeck, G.M.

BMC Microbiol.

12

126

724722

23220587

Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition

2013

Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.

Chem. Biol. Interact.

202

78-84

725133

23639754

Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes

2013

Rivera-Perez, C.; Nouzova, M.; Clifton, M.E.; Garcia, E.M.; Leblanc, E.; Noriega, F.G.

Insect Biochem. Mol. Biol.

43

675-682

726463

23229889

Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium

2013

Zheng, H.; Beliavsky, A.; Tchigvintsev, A.; Brunzelle, J.S.; Brown, G.; Flick, R.; Evdokimova, E.; Wawrzak, Z.; Mahadevan, R.; Anderson, W.F.; Savchenko, A.; Yakunin, A.F.

Proteins

81

1031-1041

726548

24490119

Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes

2013

Aukema, K.G.; Makris, T.M.; Stoian, S.A.; Richman, J.E.; Muenck, E.; Lipscomb, J.D.; Wackett, L.P.

ACS Catal.

3

2228-2238

726764

22075632

Luciferase and fluorescent protein as dual reporters analyzing the effect of n-dodecyltrimethylammonium bromide on the physiology of Pseudomonas putida

2012

Zhang, C.; Su, F.Y.; Zhang, J.F.; Yan, S.T.; Xing, X.H.

Appl. Microbiol. Biotechnol.

93

393-400

727031

24004065

The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion

2013

Tinikul, R.; Pitsawong, W.; Sucharitakul, J.; Nijvipakul, S.; Ballou, D.P.; Chaiyen, P.

Biochemistry

52

6834-6843

728228

23616465

Coexpression of luxA and luxB genes of Vibrio fischeri in NIH3T3 mammalian cells and evaluation of its bioluminescence activities

2014

Tehrani, G.A.; Mirzaahmadi, S.; Bandehpour, M.; Kazemi, B.

Luminescence

29

13-19

728284

-

Trigger factor-dependent refolding of bacterial luciferases in Escherichia coli: Kinetics, efficiency, and effect of bichaperone system

2013

Melkina, O.; Goryanin, I.; Manukhov, I.; Zavilgelskii, G.

Mol. Biol.

47

435-439

728435

21913926

Activities, kinetics and emission spectra of bacterial luciferase-fluorescent protein fusion enzymes

2011

Ke, D.; Tu, S.C.

Photochem. Photobiol.

87

1346-1353

742258

23220587

Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition

2013

Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.

Chem. Biol. Interact.

202

78-84

742654

23639754

Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes

2013

Rivera-Perez, C.; Nouzova, M.; Clifton, M.E.; Garcia, E.M.; LeBlanc, E.; Noriega, F.G.

Insect Biochem. Mol. Biol.

43

675-682

744492

28126438

Synthesis of alpha,beta-unsaturated aldehydes as potential substrates for bacterial luciferases

2017

Brodl, E.; Ivkovic, J.; Tabib, C.R.; Breinbauer, R.; Macheroux, P.

Bioorg. Med. Chem.

25

1487-1495

744675

26896339

Discovery of new substrates for LuxAB bacterial bioluminescence

2016

Jiang, T.; Wang, W.; Wu, X.; Wu, W.; Bai, H.; Ma, Z.; Shen, Y.; Yang, K.; Li, M.

Chem. Biol. Drug Des.

88

197-208

747351

27588038

Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length

2016

Bao, L.; Li, J.J.; Jia, C.; Li, M.; Lu, X.

Biotechnol. Biofuels

9

185

748027

26284355

Rapid reduction of the diferric-peroxyhemiacetal intermediate in aldehyde-deformylating oxygenase by a cyanobacterial ferredoxin evidence for a free-radical mechanism

2015

Rajakovich, L.J.; N?rgaard, H.; Warui, D.M.; Chang, W.C.; Li, N.; Booker, S.J.; Krebs, C.; Bollinger, J.M.; Pandelia, M.E.

J. Am. Chem. Soc.

137

11695-11709

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