Reference to 4.1.99.5; Id = 749051 - BRENDA Enzyme Database

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

pentadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

pentadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme

heptadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

heptadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme

1-heptadecene + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

1-heptadecene + formate + H2O + 2 NADP+

-

?

aldehyde deformylating oxygenase

-

Nostoc punctiforme

Npun_R1711

-

Nostoc punctiforme

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

pentadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

pentadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme

heptadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

heptadecane + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme

1-heptadecene + formate + H2O + 2 NADP+

-

?

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

-

749051

Nostoc punctiforme ATCC 29133 / PCC 73102

1-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 = FACHB-805, Synechocystis sp. PCC 6803, Synechococcus elongatus PCC 7942 = FACHB-805 R2

BMC Biotechnol.

17

31-39

2017

-

21

-

9

-

2

-

3

-

13

-

11

1

7

-

29

-

1

-

1

-

21

-

9

-

2

-

3

-

11

1

-

29

-

2

-

9

748564

Patrikainen

Comparison of orthologous cya ...

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

Metab. Eng. Commun.

5

9-18

2017

-

4

-

5

-

6

-

13

-

30

-

14

-

4

-

4

-

5

-

6

-

30

-

746976

Park

Crystal structures of aldehyd ...

Oscillatoria sp. KNUA011, Limnothrix redekei, Limnothrix redekei KNUA012

Biochem. Biophys. Res. Commun.

477

395-400

2016

-

2

-

3

-

7

-

6

2

4

2

-

2

-

2

-

2

-

3

-

6

2

-

2

-

4

-

747351

Bao

Structure-oriented substrate ...

Synechococcus elongatus PCC 7942 = FACHB-805, Synechococcus elongatus PCC 7942 = FACHB-805 R2

Biotechnol. Biofuels

9

185

2016

-

1

-

13

-

7

-

2

-

7

-

1

-

14

-

6

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

-

8

-

4

-

3

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

-

11

-

2

-

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

-

9

-

1

-

10

-

2

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

-

7

-

1

-

8

1

3

-

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

-

8

-

1

-

10

-

2

1

-

5

-

1

-

1

-

8

-

1

-

1

-

2

-

1

-

10

-

1

-

5

-

3

-

749212

Jia

Structural insights into the ...

Synechococcus elongatus PCC 7942 = FACHB-805, Synechococcus elongatus PCC 7942 = FACHB-805 R2

Protein Cell

6

55-67

2015

-

1

3

-

1

-

2

-

6

-

1

-

6

1

5

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

-

3

-

1

-

6

-

3

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

-

4

-

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

-

2

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

-

3

1

-

1

-

1

-

1

-

1

-

8

-

1

-

1

-

727215

Zhang

Conversion of fatty aldehydes ...

Synechococcus elongatus, Synechococcus elongatus PCC 7942

Biotechnol. Biofuels

6

86

2013

-

1

-

1

-

1

2

-

5

-

1

-

10

1

3

1

-

1

-

3

-

1

3

-

1

-

1

2

-

1

-

10

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

-

3

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

-

3

-

1

-

2

-

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

-

2

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

-

2

-

1

-

2

-

5

-

1

-

4

-

2

1

-

1

-

2

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

-

1

-

726957

Eser

Oxygen-independent alkane form ...

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

Biochemistry

50

10743-10750

2011

-

4

-

4

-

9

-

4

-

15

-

8

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

-

1

-

648395

Schneider-Belhaddad

Solubilization, partial purifi ...

Pisum sativum

Arch. Biochem. Biophys.

377

341-349

2000

4

-

7

-

2

1

-

8

1

-

1

-

1

-

2

1

-

1

-

4

-

9

-

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

-

6

-

1

-

1

-

4

1

-

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

-

4

-

2

-

2

-

1

-

1

-

1

-

1

-

1

-

2

-

6

-

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: