BRENDA - Reference to 4.1.99.5; Id = 749051

recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS

Nostoc punctiforme

C107A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C107A/C117A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C117A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C71A

site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme

Nostoc punctiforme

C71A/C107A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71A/C107A/C117A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71A/C117A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71S

site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme

Nostoc punctiforme

additional information

-

additional information

Michaelis-Menten kinetics

Nostoc punctiforme

Fe2+

di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme

Nostoc punctiforme

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

Nostoc punctiforme

-

an alkane + formate + H2O + 2 NADP+

-

?

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

Nostoc punctiforme ATCC 29133 / PCC 73102

-

an alkane + formate + H2O + 2 NADP+

-

?

Nostoc punctiforme

B2J1M1

-

Nostoc punctiforme ATCC 29133 / PCC 73102

B2J1M1

-

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis

Nostoc punctiforme

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

an alkane + formate + H2O + 2 NADP+

-

?

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

an alkane + formate + H2O + 2 NADP+

-

?

additional information

GC-MS measurements and identification of products

749051

Nostoc punctiforme

?

-

additional information

GC-MS measurements and identification of products

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

?

-

n-hexadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-pentadecane + formate + H2O + 2 NADP+

-

?

n-hexadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-pentadecane + formate + H2O + 2 NADP+

-

?

n-octadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-heptadecane + formate + H2O + 2 NADP+

-

?

n-octadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-heptadecane + formate + H2O + 2 NADP+

-

?

n-octadecenal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-heptadecene + formate + H2O + 2 NADP+

-

?

n-octadecenal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-heptadecene + formate + H2O + 2 NADP+

-

?

37

-

in vivo assay at

Nostoc punctiforme

43

-

Tm of recombinant mutant C107A/C117A

Nostoc punctiforme

46

-

Tm of recombinant mutant C71S

Nostoc punctiforme

47

-

Tm of recombinant mutants C71A, C107A, C117A, and C71A/C117A

Nostoc punctiforme

48

-

Tm of recombinant mutant C71A/C107A

Nostoc punctiforme

53

-

Tm of recombinant wild-type

Nostoc punctiforme

NADPH

-

Nostoc punctiforme

recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS

Nostoc punctiforme

NADPH

-

Nostoc punctiforme

C107A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C107A/C117A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C117A

site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme

Nostoc punctiforme

C71A

site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme

Nostoc punctiforme

C71A/C107A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71A/C107A/C117A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71A/C117A

site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant

Nostoc punctiforme

C71S

site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme

Nostoc punctiforme

additional information

-

additional information

Michaelis-Menten kinetics

Nostoc punctiforme

Fe2+

di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme

Nostoc punctiforme

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

Nostoc punctiforme

-

an alkane + formate + H2O + 2 NADP+

-

?

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

Nostoc punctiforme ATCC 29133 / PCC 73102

-

an alkane + formate + H2O + 2 NADP+

-

?

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis

Nostoc punctiforme

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

an alkane + formate + H2O + 2 NADP+

-

?

a long-chain aldehyde + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

an alkane + formate + H2O + 2 NADP+

-

?

additional information

GC-MS measurements and identification of products

749051

Nostoc punctiforme

?

-

additional information

GC-MS measurements and identification of products

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

?

-

n-hexadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-pentadecane + formate + H2O + 2 NADP+

-

?

n-hexadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-pentadecane + formate + H2O + 2 NADP+

-

?

n-octadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-heptadecane + formate + H2O + 2 NADP+

-

?

n-octadecanal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-heptadecane + formate + H2O + 2 NADP+

-

?

n-octadecenal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme

n-heptadecene + formate + H2O + 2 NADP+

-

?

n-octadecenal + O2 + 2 NADPH + 2 H+

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

n-heptadecene + formate + H2O + 2 NADP+

-

?

37

-

in vivo assay at

Nostoc punctiforme

43

-

Tm of recombinant mutant C107A/C117A

Nostoc punctiforme

46

-

Tm of recombinant mutant C71S

Nostoc punctiforme

47

-

Tm of recombinant mutants C71A, C107A, C117A, and C71A/C117A

Nostoc punctiforme

48

-

Tm of recombinant mutant C71A/C107A

Nostoc punctiforme

53

-

Tm of recombinant wild-type

Nostoc punctiforme

malfunction

C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview

Nostoc punctiforme

additional information

Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme

Nostoc punctiforme

physiological function

aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria

Nostoc punctiforme

malfunction

C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview

Nostoc punctiforme

additional information

Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme

Nostoc punctiforme

physiological function

aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria

Nostoc punctiforme

747409

Wang

Identification of residues im ...

Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2, Synechocystis sp. PCC 6803

BMC Biotechnol.

17

31-39

2017

-

21

-

8

-

2

-

3

-

9

-

11

1

-

28

-

1

-

1

-

21

-

8

-

2

-

3

-

11

1

-

28

-

2

-

9

748564

Patrikainen

Comparison of orthologous cya ...

Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102, Prochlorococcus marinus, Prochlorococcus marinus MIT 9313, Synechococcus sp. RS9917, Synechocystis sp. PCC 6803

Metab. Eng. Commun.

5

9-18

2017

-

4

-

5

-

6

-

13

-

30

-

4

-

4

-

5

-

6

-

30

-

746976

Park

Crystal structures of aldehyd ...

Limnothrix redekei, Limnothrix redekei KNUA012, Oscillatoria sp. KNUA011

Biochem. Biophys. Res. Commun.

477

395-400

2016

-

2

-

3

-

5

-

6

2

-

2

-

2

-

2

-

3

-

6

2

-

2

-

4

-

747351

Bao

Structure-oriented substrate ...

Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2

Biotechnol. Biofuels

9

185

2016

-

1

-

13

-

7

-

2

-

6

-

1

-

14

-

1

-

8

1

-

1

-

1

-

13

-

7

-

2

-

1

-

14

-

1

-

8

1

-

2

-

8

747353

Zhang

Microbial synthesis of propan ...

Prochlorococcus marinus, Prochlorococcus marinus MIT 9313

Biotechnol. Biofuels

9

80

2016

-

1

-

3

-

2

-

7

-

4

-

1

-

1

-

1

-

3

-

2

-

4

-

1

-

1

-

747081

Warui

Efficient delivery of long-ch ...

Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102

Biochemistry

54

1006-1015

2015

-

2

-

9

-

2

-

1

-

1

-

2

-

2

-

2

-

748027

Rajakovich

Rapid reduction of the diferr ...

Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102

J. Am. Chem. Soc.

137

11695-11709

2015

-

1

-

2

-

8

-

1

-

10

-

1

-

1

-

2

-

2

-

1

-

2

-

10

-

1

-

1

-

1

-

748032

Shokri

Conversion of aldehyde to alk ...

Prochlorococcus marinus, Prochlorococcus marinus MIT 9313

J. Am. Chem. Soc.

137

7686-7691

2015

-

1

-

1

-

2

-

6

-

1

-

8

1

-

1

-

1

-

1

-

1

-

2

-

8

1

-

2

-

749051

Hayashi

Role of cysteine residues in ...

Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102

PLoS ONE

10

e0122217

2015

-

1

-

8

-

1

-

1

-

2

-

7

-

1

-

10

-

1

-

5

-

1

-

1

-

8

-

1

-

1

-

2

-

1

-

10

-

1

-

5

-

3

-

749212

Jia

Structural insights into the ...

Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2

Protein Cell

6

55-67

2015

-

1

3

-

1

-

2

-

6

-

1

-

6

1

-

1

-

1

-

1

3

-

1

-

2

-

1

-

6

1

-

1

-

4

-

726552

Das

Mechanistic insights from reac ...

Nostoc punctiforme

ACS Chem. Biol.

9

570-577

2014

-

1

-

1

-

1

-

1

-

2

-

1

-

6

-

1

-

3

1

-

2

-

1

2

-

1

-

1

-

1

-

1

-

6

-

1

-

3

1

-

1

-

746597

Buer

Insights into substrate and m ...

Prochlorococcus marinus, Prochlorococcus marinus MIT 9313

ACS Chem. Biol.

9

2584-2593

2014

-

1

-

1

-

1

-

2

-

6

-

1

-

8

-

1

-

1

-

1

-

1

-

1

-

2

-

8

-

1

-

2

-

747074

Waugh

Solvent isotope effects on al ...

Prochlorococcus marinus, Prochlorococcus marinus MIT9313

Biochemistry

53

5537-5543

2014

-

1

-

1

-

1

-

2

1

3

-

1

-

6

-

1

-

1

-

1

-

1

-

1

-

1

-

2

1

-

1

-

6

-

1

-

1

-

1

-

726548

Aukema

Cyanobacterial aldehyde deform ...

Prochlorococcus marinus, Prochlorococcus marinus MIT 9313

ACS Catal.

3

2228-2238

2013

-

1

-

6

-

1

-

8

-

1

-

1

-

1

-

1

-

1

-

8

-

1

-

1

-

727215

Zhang

Conversion of fatty aldehydes ...

Synechococcus elongatus

Biotechnol. Biofuels

6

86

2013

-

1

-

1

-

1

-

3

-

1

-

5

1

-

1

-

3

-

1

3

-

1

-

1

-

1

-

5

1

-

1

-

727312

Khara

Production of propane and othe ...

Prochlorococcus marinus, Prochlorococcus marinus MIT9313

ChemBioChem

14

1204-1208

2013

-

1

-

4

-

1

-

2

-

3

-

1

-

8

-

1

-

1

-

1

-

1

-

4

-

1

-

2

-

1

-

8

-

1

-

1

-

1

-

727690

Pandelia

Substrate-triggered addition o ...

Nostoc punctiforme

J. Am. Chem. Soc.

135

15801-15812

2013

1

-

1

-

1

-

1

-

1

-

2

-

1

-

2

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

2

-

1

-

1

-

727693

Paul

Probing the mechanism of cyano ...

Nostoc punctiforme

J. Am. Chem. Soc.

135

5234-5237

2013

-

1

-

1

-

3

-

1

-

1

-

1

-

1

-

1

-

3

-

1

-

1

-

727001

Li

Evidence for only oxygenative ...

Prochlorococcus marinus

Biochemistry

51

7908-7916

2012

-

1

-

4

-

3

-

1

-

1

-

1

-

3

-

1

-

1

-

1

-

715293

Warui

Detection of formate, rather t ...

Nostoc punctiforme

J. Am. Chem. Soc.

133

3316-3319

2011

-

1

-

1

-

2

-

4

-

1

-

4

-

1

-

1

-

1

-

1

-

2

-

1

-

4

-

1

-

1

-

715300

Li

Conversion of fatty aldehydes ...

Nostoc punctiforme

J. Am. Chem. Soc.

133

6158-6161

2011

-

1

-

2

-

1

-

1

-

1

-

1

-

1

-

726957

Eser

Oxygen-independent alkane form ...

Nostoc punctiforme, Prochlorococcus marinus, Prochlorococcus marinus MIT9313, Synechococcus sp., Synechocystis sp.

Biochemistry

50

10743-10750

2011

-

4

-

4

-

8

-

4

-

15

-

4

-

4

-

4

-

4

-

4

-

15

-

4

-

4

-

4

-

713511

Schirmer

Microbial biosynthesis of alka ...

Nostoc punctiforme

Science

329

559-562

2010

-

1

-

3

-

1

-

1

-

1

-

1

-

1

-

1

-

648395

Schneider-Belhaddad

Solubilization, partial purifi ...

Pisum sativum

Arch. Biochem. Biophys.

377

341-349

2000

4

-

7

-

2

1

-

4

1

-

1

-

1

-

2

1

-

4

-

7

-

2

1

-

1

-

1

-

1

-

2

1

-

648396

Kobayashi

Cobalt proteins ...

Botryococcus braunii

Eur. J. Biochem.

261

1-9

1999

-

1

2

1

-

1

-

2

1

-

1

2

1

-

2

1

-

648394

Dennis

A cobalt-porphyrin enzyme conv ...

Botryococcus braunii, Botryococcus braunii Austin

Proc. Natl. Acad. Sci. USA

89

5306-5310

1992

-

1

-

1

2

-

5

-

1

-

1

-

4

1

-

1

-

1

2

-

1

-

1

-

4

1

-

648393

Dennis

Alkane biosynthesis by decarbo ...

Botryococcus braunii, Botryococcus braunii Austin

Arch. Biochem. Biophys.

287

268-275

1991

1

-

5

1

2

1

-

2

-

6

1

-

4

-

1

-

1

-

1

-

1

-

1

-

1

-

5

-

1

2

1

-

2

-

1

-

4

-

1

-

1

-

1

-

648392

Cheesbrough

Microsomal preparation from an ...

Podiceps nigricollis

J. Biol. Chem.

263

2738-2743

1988

2

-

9

1

2

1

-

1

-

3

1

-

1

-

2

-

1

-

1

-

1

-

1

-

2

-

1

-

9

-

1

2

1

-

1

-

1

-

1

-

2

-

1

-

1

-

1

-

648391

Cheesbrough

Alkane biosynthesis by decarbo ...

Pisum sativum

Proc. Natl. Acad. Sci. USA

81

6613-6617

1984

-

2

4

1

-

1

-

3

-

2

-

2

-

1

-

1

-

1

-

1

-

1

-

2

-

4

-

1

-

1

-

2

-

2

-

1

-

1

-

1

-

Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase

Data extracted from this reference: