Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase

Substrates: 792% relative activity compared to acetophenone
Products: -

?

2',3',4',5',6'-pentafluoroacetophenone + NADPH

? + NADP+

Substrates: 3023% relative activity compared to acetophenone
Products: -

?

2-octanone + NADPH

? + NADP+

Substrates: 15% relative activity compared to acetophenone
Products: -

?

3'-fluoroacetophenone + NADPH

? + NADP+

Substrates: 100% relative activity compared to acetophenone
Products: -

?

3-hydroxydecanoyl-N-acetylcysteamine + NADP+

3-oxodecanoyl-N-acetylcysteamine + NADPH + H+

O54438

739774

Substrates: -
Products: -

?

3-oxoacyl-[acyl-carrier protein] + NADPH

(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

24 entries

3-oxoacyl-[acyl-carrier protein] + NADPH

3-hydroxyacyl-[acyl-carrier protein] + NADP+

3-oxoacyl-[acyl-carrier protein] + NADPH + H+

(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

3-oxobutyryl-[acyl-carrier protein] + NADPH

(R)-3-hydroxybutyryl-[acyl-carrier protein] + NADP+

-

763418, 763477

Substrates: weak activity
Products: -

?

3-oxodecanoyl-CoA + NADPH

(R)-3-hydroxydecanoyl-CoA + NADP+

3-oxodecanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxydecanoyl-[acyl-carrier protein] + NADP+

3-oxododecanoyl-CoA + NADPH

(R)-3-hydroxydodecanoyl-CoA + NADP+

3-oxododecanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxydodecanoyl-[acyl-carrier protein] + NADP+

3-oxohexadecanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxyhexadecanoyl-[acyl-carrier protein] + NADP+

3-oxohexanoyl-CoA + NADH + H+

(3R)-3-hydroxyhexanoyl-CoA + NAD+

3-oxohexanoyl-CoA + NADPH

(R)-3-hydroxyhexanoyl-CoA + NADP+

3-oxohexanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxyhexanoyl-[acyl-carrier protein] + NADP+

-

763418, 763477

Substrates: weak activity
Products: -

?

3-oxooctanoyl-CoA + NADPH

(R)-3-hydroxyoctanoyl-CoA + NADP+

3-oxooctanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxyoctanoyl-[acyl-carrier protein] + NADP+

3-oxotetradecanoyl-[acyl-carrier protein] + NADPH

(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + NADP+

4'-chloroacetophenone + NADPH

? + NADP+

Substrates: 115% relative activity compared to acetophenone
Products: -

?

4'-fluoroacetophenone + NADPH

? + NADP+

Substrates: 62% relative activity compared to acetophenone
Products: -

?

9,10-phenanthrene quinone + NADH + H+

?

Substrates: -
Products: -

?

9,10-phenanthrene quinone + NADPH + H+

?

Substrates: low activity with NADPH
Products: -

?

a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

acetoacetyl-CoA + NADH + H+

?

Substrates: -
Products: -

?

acetoacetyl-CoA + NADPH

3-hydroxybutyryl-CoA + NADP+

acetoacetyl-CoA + NADPH

? + NADP+

-

Substrates: wild-type shows less activity with acetoacetyl-CoA than with acetoacetyl-[acyl-carrier protein]
Products: -

?

acetoacetyl-CoA + NADPH + H+

3-hydroxybutyryl-CoA + NADP+

13 entries

acetoacetyl-CoA + NADPH + H+

?

acetoacetyl-CoA + NADPH + H+

D-3-hydroxybutyryl-CoA + NADP+

-

Substrates: -
Products: -

?

acetoacetyl-CoA + NADPH + H+

D-beta-hydroxybutyryl-CoA + NADP+

acetoacetyl-N-acetylcysteamine + NADPH + H+

D-3-hydroxybutyryl-N-acetylcysteamine + NADP+

-

Substrates: -
Products: -

r

acetoacetyl-N-cysteamine + NADPH

D-3-hydroxybutyryl-N-cysteamine + NADP+

acetoacetyl-[acyl-carrier protein] + NADPH

D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+

11 entries

acetophenone + NADPH

? + NADP+

Substrates: 100% relative activity
Products: -

?

alpha-chloroacetophenone + NADPH

? + NADP+

Substrates: 1885% relative activity compared to acetophenone
Products: -

?

beta-ketoacyl-[acyl-carrier protein] + NADPH

beta-hydroxyacyl-[acyl-carrier protein] + NADP+

beta-ketoacyl-[acyl-carrier protein] + NADPH + H+

beta-hydroxyacyl-[acyl-carrier protein] + NADP+

beta-ketobutyryl-CoA + NADPH

beta-hydroxybutyryl-CoA + NADP+

Lactococcus lactis

-

654725

Substrates: complementation of Escherichia coli fabG mutant with Lactobacillus lactis fabG genes shows that fabG1 encodes a functional beta-ketoacyl ACP reductase and fabG2 encodes an enzyme that has activity with the model substrate beta-ketobutyryl-CoA, but lacks the ability to support fatty acid synthesis both in vivo and in vitro
Products: -

?

ethyl 4-chloroacetoacetate + NADPH

? + NADP+

Substrates: 29454% relative activity compared to acetophenone
Products: -

?

ethyl acetoacetate + NADPH

? + NADP+

-

Substrates: -
Products: -

?

ethyl acetoacetate + NADPH

ethyl 3-hydroxybutyrate + NADP+

ethylbenzoylacetate + NADPH

? + NADP+

Substrates: 892% relative activity compared to acetophenone
Products: -

?

methyl acetoacetate + NADPH

? + NADP+

-

Substrates: is not a good substrate as ethyl acetoacetate
Products: -

?

propiophenone + NADPH

? + NADP+

Substrates: 123% relative activity compared to acetophenone
Products: -

?

propyl acetoacetate + NADPH

? + NADP+

-

Substrates: as substrate it is limited to its weak solubility
Products: -

?

additional information

?

-

28 entries

(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

3-oxoacyl-[acyl-carrier protein] + NADPH + H+

Pseudomonas putida

A5HIF6

693287

Substrates: beta-oxidation pathway
Products: -

?

3-oxoacyl-[acyl-carrier protein] + NADPH

(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

3-oxoacyl-[acyl-carrier protein] + NADPH

3-hydroxyacyl-[acyl-carrier protein] + NADP+

3-oxoacyl-[acyl-carrier protein] + NADPH + H+

(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

-

Substrates: -
Products: -

?

a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+

a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

acetoacetyl-CoA + NADPH

3-hydroxybutyryl-CoA + NADP+

-

Substrates: -
Products: -

?

acetoacetyl-CoA + NADPH + H+

3-hydroxybutyryl-CoA + NADP+

beta-ketoacyl-[acyl-carrier protein] + NADPH

beta-hydroxyacyl-[acyl-carrier protein] + NADP+

beta-ketoacyl-[acyl-carrier protein] + NADPH + H+

beta-hydroxyacyl-[acyl-carrier protein] + NADP+

additional information

?

-

NADH

NADP+

NADPH

additional information

-

additional information

(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one

80% residual activity

(E)-2-nitrophenyl cinnamate

-

(E)-3-phenoxybenzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

61% residual activity

(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

-

(E)-benzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

71% residual activity

(E)-phenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

69% residual activity

1,2,3,4,6-penta-O-galloyl-beta-D-glucose

3-hydroxybutyryl-CoA

4-acetoxyanthecotulide

-

most active linear sesquiterpene lactone from Anthemis auriculata against FabG

4-hydroxyanthecotulide

-

linear sesquiterpene lactone from Anthemis auriculata

Acyl carrier protein

Lactococcus lactis

-

beta-ketobutyryl-CoA reductase activity of FabG1 is inhibited, activity of FabG2 is unaffected

654725

acyl-carrier protein

-

inhibition of wild-type with increasing concentrations

anthecotulide

-

linear sesquiterpene lactone from Anthemis auriculata

bithionol

over 75% inhibition at 0.02 mM, IC50: 0.010 mM

bromochlorophen

an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM

chlorogenic acid

-

IC50: 0.881-0.948 mM

di-resorcinol sulfide

over 75% inhibition at 0.02 mM, IC50: 0.0038 mM

DL-3-hydroxybutyryl-CoA

-

competitive product inhibition

epigallocatechin gallate

-

grape skin extract

Gallus gallus

-

inhibits the overall reaction and beta-ketoacyl reductase reaction of FAS with IC50 values of 4.61 microg/ml and 20.3 microg/ml, respectively. Inhibits the overall reaction of FAS competitively with acetyl-CoA, noncompetitively with malonyl-CoA and in a mixed manner with NADPH

735850

-

Guanidinium chloride

-

FabG is fully unfolded at 4 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. In presence of NADPH, there is no stabilization of FabG in case of equilibrium unfolding with guanidinium chloride

706639

Hexachlorophene

an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM

kaempferol

synthetic construct

-

N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide

69% residual activity

NADP+

p-chloromercuribenzoate

-

Phenylglyoxal

quercetin

resveratrol

-

inhibits the overall reaction and beta-ketoacyl reductase reaction of FAS with IC50 values of 11.1 microg/ml and 21.9 microg/ml, respectively. In 3 T3-L1 preadipocytes, resveratrol reduces lipid accumulation remarkably

735850

RNAi

-

suppresses KCR activity, which results in a reduction of cuticular wax load and affects very-long-chain fatty acid composition of sphingolipids, seed triacylglycerols, and root glycerolipids. RNAi-suppressed Arabidopsis KCR1 plants display fused vegetative and reproductive organs, an abnormal root morphology and have abnormal trichome and epidermal cell morphology

700827

-

tachyplesin

-

Tannic acid

16 entries

Urea

-

FabG is fully unfolded at 6 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. Two states in the reversible unfolding process of FabG in presence of NADPH, one is an activity-enhanced state and the other, an inactive state in case of equilibrium unfolding with urea

706639

additional information

26 entries

-

additional information

-

89.2

1,1,1-trifluoroacetone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

5.72

2',3',4',5',6'-pentafluoroacetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

7.38

3'-fluoroacetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.142

3-oxododecanoyl-[acyl-carrier protein]

-

pH and temperature not specified in the publication

0.6

3-oxooctanoyl-CoA

pH 7.0, 25°C

14.34

4'-chloroacetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

12.29

4'-fluoroacetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.0057 - 3.5

acetoacetyl-CoA

23 entries

48

acetoacetyl-N-acetylcysteamine

-

0.003 - 0.017

acetoacetyl-[acyl-carrier protein]

5 entries

46.92

acetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

2.71

alpha-chloroacetophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.29 - 4.06

beta-ketobutyryl-CoA

8.31

ethyl 4-chloroacetoacetate

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.127

ethyl acetoacetate

-

1.92

ethylbenzoylacetate

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.035

N-(2-sulfanylethyl)acetamide

-

0.29

NADP+

O54438

with 3-hydroxydecanoyl-N-acetylcysteamine as cosubstrate, pH and temperature not specified in the publication

739774

0.0093 - 0.617

NADPH

21 entries

6.03

propiophenone

with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

additional information

7 entries

-

40.9

3-oxododecanoyl-[acyl-carrier protein]

-

pH and temperature not specified in the publication

0.095

3-oxooctanoyl-CoA

pH 7.0, 25°C

0.014 - 361

acetoacetyl-CoA

12 entries

0.3

ethyl acetoacetate

-

0.59 - 361

NADPH

15 entries

15200 - 26500

acetoacetyl-CoA

585 - 862

NADPH

0.0102

3-hydroxybutyryl-CoA

pH 6.8, 25°C, recombinant enzyme

additional information

-

0.45

(E)-2-nitrophenyl cinnamate

Escherichia coli

pH 7.0

0.18

(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

Escherichia coli

pH 7.0

0.18

(E)-phenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate

Escherichia coli

pH 7.0

0.5

4-acetoxyanthecotulide

Plasmodium falciparum K1

-

pH 7.0, 25°C

0.75

4-hydroxyanthecotulide

Plasmodium falciparum K1

-

pH 7.0, 25°C

1

anthecotulide

Plasmodium falciparum K1

-

pH 7.0, 25°C

0.01

bithionol

Plasmodium falciparum

over 75% inhibition at 0.02 mM, IC50: 0.010 mM

0.0154

bromochlorophen

Plasmodium falciparum

an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM

0.881 - 0.948

chlorogenic acid

Escherichia coli

-

IC50: 0.881-0.948 mM

0.0038

di-resorcinol sulfide

Plasmodium falciparum

over 75% inhibition at 0.02 mM, IC50: 0.0038 mM

0.00554 - 0.1223

epigallocatechin gallate

7 entries

0.002

Hexachlorophene

Plasmodium falciparum

an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM

0.0212

kaempferol

synthetic construct

-

pH 7.0

0.215

N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide

Escherichia coli

pH 7.0

0.3048

quercetin

synthetic construct

-

pH 7.0

0.00078

Tannic acid

Escherichia coli

-

additional information

grape skin extract

-

0.00009

-

substrate: 3-oxohexanoyl-[acyl-carrier protein], pH and temperature not specified in the publication

0.0001

-

substrate: 3-oxobutyryl-[acyl-carrier protein], pH and temperature not specified in the publication

0.0017 - 0.0018

-

recombinant refolded enzyme

0.0019

-

recombinant soluble enzyme

0.0032

-

0.00361

-

substrate: 3-oxooctanoyl-[acyl-carrier protein], pH and temperature not specified in the publication

0.00421

-

substrate: 3-oxohexadecanoyl-[acyl-carrier protein], pH and temperature not specified in the publication

0.00456

-

substrate: 3-oxotetradecanoyl-[acyl-carrier protein], pH and temperature not specified in the publication

0.005

-

0.00851

-

substrate: 3-oxododecanoyl-[acyl-carrier protein], pH and temperature not specified in the publication

0.0132

-

0.0168

-

0.0189

-

0.0192

-

0.0197

0.02

with 2-octanone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.0366

-

0.06

mutant enzyme K173A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

0.08

with 4'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.13

0.15

with 4'-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.16

with propiophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

0.44

0.46

mutant enzyme K152A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

0.5

mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

0.65

mutant enzyme Y169A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

0.85

mutant enzyme Y169A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

1.03

with 1,1,1-trifluoroacetone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

1.16

with ethylbenzoylacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

1.2

mutant enzyme K173A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

1.3

mutant enzyme K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

1.6

mutant enzyme R168E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

1.7

mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

136000

-

purified enzyme, protein determination by calculation from absorption at 280 nm

14.8

mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

15.7

mutant enzyme K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

17.4

mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

180400

-

recombinant protein, cosubstrate NADPH, pH 7.0, phosphate buffer

19.3

mutant enzyme K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

2

2.4

mutant enzyme K173A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

2.45

with alpha-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

2.6

wild type enzyme, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

20

mutant enzyme D42A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

20.5

wild type enzyme, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

20.7

mutant enzyme R34A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

20.8

wild type enzyme, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

21

mutant enzyme R34A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

21.7

mutant enzyme R168E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

22

mutant enzyme K152A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

25.5

mutant enzyme K152A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

280

-

acetoacetyl-N-acetylcysteamine

3

-

mutant R187A/R230A, acyl-carrier protein-dependent spectroscopic assay

3.1

mutant enzyme Y169A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

3.5

wild type enzyme, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

3.93

with 2',3',4',5',6'-pentafluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

31.8

mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

38.29

with ethyl 4-chloroacetoacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

3839

-

recombinant protein, cosubstrate NADH, pH 7.0, phosphate buffer

4

-

mutant R230E, acyl-carrier protein-dependent spectroscopic assay

4.3

mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

4.5

mutant enzyme K173A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

42.6

-

mutant R187E/R230E, acyl-carrier protein-independent spectroscopic assay

45.6

-

mutant R187A/R230A, acyl-carrier protein-independent spectroscopic assay

450

-

acetoacetyl-CoA

4930

-

purified enzyme

285672

5.4

mutant enzyme D42A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C

5.5

mutant enzyme K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C

530

-

acetoacteyl-ACP

54.2

-

mutant R230E, acyl-carrier protein-independent spectroscopic assay

54.5

-

mutant R187E, acyl-carrier protein-independent spectroscopic assay

55.3

-

mutant R230A, acyl-carrier protein-independent spectroscopic assay

57.9

-

mutant R187A, acyl-carrier protein-independent spectroscopic assay

59.8

6.1

-

mutant R230A, acyl-carrier protein-dependent spectroscopic assay

6.3

6.9

-

mutant R187A, acyl-carrier protein-dependent spectroscopic assay

7.3

mutant enzyme D42A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C

7.9

mutant enzyme R168E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

7.95

-

70.6

-

wild-type, acyl-carrier protein-dependent spectroscopic assay

74.6

mutant enzyme D42A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

8.4

mutant enzyme Q126E/R168E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C

83140

-

cosubstrate NADPH, pH 8.35, carbonate buffer

9401

-

purified enzyme, protein determination by amino acid analysis

additional information

5.7 - 6.2

-

6 - 7

-

6.5

-

6.8

7

7.5

-

assay at

7.6

-

8

additional information

-

increase in alpha-secondary deuterium kinetic isotope effect values measured at pH 10 as compared to those obtained at pH 7 points to isotope- and pH-sensitive steps occurring concomitantly

684702

4 - 10

pH 4: about 60% of maximal activity, pH 10: about 75% of maximal activity

5.5 - 8.5

-

about 50% of activity maximum at pH 5.5 and 8.5

285678

5.5 - 9.5

-

pH profile, detailed mechanistic pH-dependence analysis, overview

5.8 - 10

-

pH profile, pH-dependence analysis, overview

667708

6 - 8.7

-

both reaction directions

22

25

30

37

-

assay at

44

-

45

-

15 - 37

-

temperature profile

667708

30 - 55

30°C: about 55% of maximal activity, 55°C: about 65% of maximal activity

4.89

calculated from sequence

5.9

predicted

Acinetobacter baumannii

-

-

Acinetobacter baumannii 1408

-

Acinetobacter calcoaceticus

-

-

Acinetobacter calcoaceticus 25001

-

-

-

isoform FabG

-

-

-

-

763622

Enterobacter cloacae 45301

UniProt

Aurantiochytrium limacinum OUC168

-

UniProt

-

Q81JG6

SwissProt

-

-

rapeseed

-

Caenorhabditis elegans

-

-

safflower

-

-

-

-

-

-

UniProt

Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1

-

UniProt

-

-

-

Haloarcula hispanica AS2049

-

Enterococcus sp.

strains ATCC29212 and 775

-

-

Uniprot

-

-

-

-

-

-

-

-

-

-

-

-

Klebsiella aerogenes 45102

-

-

Klebsiella pneumoniae

Klebsiella pneumoniae 5

-

-

ssp. lactis IL 1403

-

-

-

Mycobacterium tuberculosis CDC 1551

-

740013

O53665

UniProt

Mycobacterium tuberculosis H37Rv

-

P9WGT3

UniProt

Mycolicibacterium smegmatis ATCC 700084

-

SwissProt

Mycolicibacterium smegmatis mc(2)155 / ATCC 700084

-

UniProt

-

-

Proteus vulgaris

-

-

Pseudomonas aeruginosa ATCC 27853

ATCC27853

-

-

UniProt

strain 61-3, non-pathogenic strain from soil, gene fabG

667257

Q4AE87

SwissProt

-

UniProt

Salmonella enterica subsp. enterica serovar Typhi

-

Salmonella enterica subsp. enterica serovar Typhi H901

-

-

Salmonella enterica subsp. enterica serovar Typhimurium

-

Serratia marcescens

-

Serratia marcescens 41002

-

-

-

-

-

-

-

-

-

Shigella sonnei 51592

-

-

-

285668, 285675, 285677

-

Staphylococcus aureus

Staphylococcus aureus ATCC 25923

ATCC25923

Staphylococcus aureus NCTC 8325

-

-

Staphylococcus epidermidis

Q2FZ53

UniProt

Streptococcus sp.

alpha-haemolytic strain 32213-7 and beta-haemolytic strain 32210-20

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UniProt

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Xanthomonas campestris pv. campestris XC1

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763418, 763477

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strain KCTC1639

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KCR1 and KCR2

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KCR1 and KCR2 present in inflorescence stem

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285670, 285674, 285678

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KCR1 and KCR2

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endoplasmic reticulum

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KCR1 and KCR2

Highest Expressing Human Cell Lines

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malfunction

metabolism

Acholeplasma laidlawii PG-8A

physiological function

Bacillus anthracis str. Ames

Acinetobacter baumannii

Bacillus subtilis subsp. subtilis str. 168

Brucella abortus 2308

Brucella melitensis bv. 1 str. 16M

Brucella suis ATCC 23445

Burkholderia multivorans ATCC 17616

Burkholderia pseudomallei

Cupriavidus taiwanensis

Drosophila melanogaster

Francisella tularensis subsp. tularensis SCHU S4

Escherichia coli CFT073

Helicobacter pylori 26695

Klebsiella pneumoniae

Klebsiella pneumoniae 30684/NJST258_2

Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044

Komagataella phaffii GS115

Mus musculus

Mycobacterium tuberculosis H37Ra

Mycobacterium tuberculosis H37Rv

7 entries

Mycolicibacterium smegmatis MC2 155

Neisseria meningitidis FAM18

Paraburkholderia xenovorans LB400

Plasmodium falciparum 3D7

Pseudomonas aeruginosa PAO1

19 entries

Rickettsia felis URRWXCal2

24 entries

Saccharomyces cerevisiae S288C

Saccharopolyspora erythraea

Saccharopolyspora spinosa

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Sinorhizobium meliloti

Sinorhizobium meliloti 1021

Staphylococcus aureus subsp. aureus Mu50

Staphylococcus aureus subsp. aureus NCTC 8325

Streptomyces coelicolor A3(2)

Streptomyces venezuelae

Syntrophus aciditrophicus SB

Thermus thermophilus HB8

uncultured bacterium Bio5

Vibrio cholerae O1 biovar El Tor str. N16961

Yersinia pestis

100000

A0R723

x * 100000, SDS-PAGE

740023

102000

gel filtration

110000

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gel filtration, wild-type and mutants

116000

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recombinant enzyme, analytical ultracentrifugation, tetrameric at higher enzyme concentrations

120000

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gel filtration

130000

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gel filtration

133000

tagged enzyme form, gel filtration

24000

24200

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4 * 24200, SDS-PAGE

25000

25500

26400

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27000

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? * 27000, DNA sequence calculation

28000

29000

31000

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4 * 31000, SDS-PAGE, wild-type and mutants

35000

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sequence analysis, KCR2

700827

351500

calculated from sequence

763622

40000 - 46000

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gel filtration, sucrose density gradient centrifugation

285678

44000

Euglena gracilis

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gel filtration

285676

50400

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recombinant enzyme, gel filtration

58400

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recombinant enzyme, analytical ultracentrifugation

64000

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gel filtration

285677

97000

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gel filtration

?

dimer

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2 * 29000, recombinant enzyme, SDS-PAGE

heterotetramer

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homodimer

x-ray crystallography

homodimer or homotetramer

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2 or 4 * 25000, SDS-PAGE

homotetramer

tetramer

10 entries

additional information

additional information

diffraction to 1.8 A, determinantion of initial phases by molecular replacement

Aquifex aeolicus VF5

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684165

at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates

Bacillus anthracis

Q81JG6

706640

diffraction to 2.4 A. Final model contains two tetramers displaying 222 symmetry and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates

Q81JG6

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structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism

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285683

vapor diffusion method, using 0.1 M MES (pH 7.1), 1.6 M ammonium sulfate, and 10% (w/v) 1,4-dioxane

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sitting drop vapor diffusion method, using 15-18% (w/v) PEG3350 and 0.4 M ammonium acetate in sodium acetate buffer at pH 5.0

in complex with hexanoyl-CoA, hanging drop vapor diffusion method, using

O53665

740013

hanging drop vapor diffusion method, apoenzyme is crystallized by using 100 mM Na-HEPES (pH 7.5), 30% (w/v) PEG 400 and 200 mM magnesium chloride hexahydrate, while the complex with NADP+ is crystallized by using 200 mM sodium citrate tribasic dehydrate and 20% (w/v) PEG 3350

A0R723

740023

high-resolution crystal structures of the enzyme (MabA) in its apo, NADP+-bound and NADPH-bound forms. Crystals are grown in sitting drops in MR Crystallization Plates (Hampton Research) at 18°C

purified recombinant enzyme, vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 6.8, 0.5 M NaCl, 1 mM DTT, and 0.5 mM EDTA, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.0, 35% v/v 2-methyl-2,4-pentanediol, and 0.2 M LiSO4, equilibration against 1 ml of mother liquor, room temperature, 6 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution

purified native and selenomethionine-labeled recombinant enzyme, hanging drop vapour diffusion method, 18°C, 2.5 mg/ml protein in 50 mm HEPES, pH 7.0, 5 mM Tris, pH 8.0, 0.15 mM ammonium sulfate, 6% PEG 4000, 0.1 M NaCl, 0.5 mM EDTA, and 0.5 mM DTT, mixed with reservoir solution containing 1 M HEPES, pH 7.0, 0.3 M ammonium sulfate, and 12% PEG 4000, plus 1 mM NADPH, X-ray diffraction structure determination and analysis at 2.3 A resolution

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crystalized at a resolution of 2.25 A

apo-form complexed with NADPH, vapor diffusion method, using 10% (w/v) polyethylene glycol 4000, 10% (v/v) 2-propanol, 0.1 M HEPES pH 7.0 and 30% (v/v) jeffamine ED2001, 0.1 M HEPES pH 7.5

hanging drop vapor diffusion method, using 2.0-2.7 M ammonium sulfate and 0.1 M Tris (pH 9.0)

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Q47L

the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme

T173S

the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme

Q47L

Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1

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the mutant with increased specific activity exhibits a kcat value that is 2.4fold higher than that of the wild type enzyme

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T173S

Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1

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the mutant with increased specific activity exhibits a kcat value that is 3.5fold higher than that of the wild type enzyme

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A154T

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similar thermal stability as wild-type enzyme

A154T/E233K

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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain

E233K

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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain

F87T

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coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources

685775

D42A

the mutant shows 36% activity with acetoacetyl-CoA and NADH, 20% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 26% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

K152A

the mutant shows 109% activity with acetoacetyl-CoA and NADH, no activity with acetoacetyl-CoA and NADPH, 123% activity with 9,10-phenanthrene and NAD+, and 2.2% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

K169E

the mutant shows 95% activity with acetoacetyl-CoA and NADH, 5.5% activity with acetoacetyl-CoA and NADPH, 76% activity with 9,10-phenanthrene and NAD+, and 6% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

K173A

the mutant shows 0.3% activity with acetoacetyl-CoA and NADH, 2.4% activity with acetoacetyl-CoA and NADPH, 6% activity with 9,10-phenanthrene and NAD+, and 22% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

Q126E/K169E

the mutant shows 156% activity with acetoacetyl-CoA and NADH, 4.3% activity with acetoacetyl-CoA and NADPH, 84% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

Q126E/R168E/K169E

the mutant shows 72% activity with acetoacetyl-CoA and NADH, 0.5% activity with acetoacetyl-CoA and NADPH, 40% activity with 9,10-phenanthrene and NAD+, and no activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

R168E

the mutant shows 106% activity with acetoacetyl-CoA and NADH, 6.3% activity with acetoacetyl-CoA and NADPH, 38% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

R34A

the mutant shows 102% activity with acetoacetyl-CoA and NADH, 100% activity with acetoacetyl-CoA and NADPH, 40.44% activity with 9,10-phenanthrene and NAD+, and 2.1% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

Y169A

the mutant shows 3% activity with acetoacetyl-CoA and NADH, 2% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 15% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively

S140A

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mutant shows no enzymatic activity. S140A mutant does not bind to NADPH

S140T

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mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding

R187A

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 3fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R187A/R230A

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R187E

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 4fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R187E/R230E

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 80fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R187K

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no decreased affinity binding to acyl-carrier protein with respect to wild-type

R230A

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R230E

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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 41fold decreased affinity binding to acyl-carrier protein with respect to wild-type

R14A

inactive

S36A

the mutant shows reduced activity compared to the wild type enzyme

S40A

the mutant shows reduced activity compared to the wild type enzyme

Salmonella enterica subsp. enterica serovar Typhimurium

E233K

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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay

Salmonella enterica subsp. enterica serovar Typhimurium

M125I/S233T

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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay

G141A

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the mutant shows less than 5% of wild type activity

G92A

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the mutant shows less than 60% of wild type activity

G92D

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the mutant shows less than 5% of wild type activity

Q152A

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the mutant shows less than 10% of wild type activity

Y155F

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the mutant shows less than 3% of wild type activity

additional information

30

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wild-type enzyme: about 15% loss of activity after 15 min, mutant enzyme E233K: about 60% loss of activity after 10 min,mutant enzyme A164T: about 20% loss of activity after 15 min, mutant enzyme A154T/E233K: about 80% loss of activity after 15 min

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wild-type enzyme: about 40% loss of activity after 15 min, mutant enzyme E233K: about 90% loss of activity after 10 min, mutant enzyme A164T: about 25% loss of activity after 15 min, mutant enzyme A154T/E233K: about 80% loss of activity after 5 min

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wild-type enzyme: about 70% loss of activity after 15 min, mutant enzyme E233K: complete loss of activity after 10 min, mutant enzyme A164T: about 60% loss of activity after 15 min, mutant enzyme A154T/E233K: complete loss of activity after 5 min

inactivation by dilution can be partly prevented by inclusion of NADPH

the purified recombinant enzyme is stable at room temperature at concentrations above 0.2 mg/ml, but unstable at 0.01 mg/ml

-20°C, phosphate buffer, 10% glycerol

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-20°C, stable for 2 months

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-80°C, 10% glycerol

-80�C, 50% glycerol

27°C, 100 mM potassium phosphate buffer, 13% loss of activity after 24 h

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27°C, 2 M NaCl, 24 h stable

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4°C, 100 mM potassium phosphate, 52% loss of activity after 24 h

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10 entries

by gel filtration and ion exchange chromatography, to homogeneity

by nickel affinity chromatography

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by nickel chelation affinity chromatography

by nickel-affinity chromatography

Bacillus anthracis

Q81JG6

706640

by sonication, centrifugation and on Ni-NTA column

His-Bind resin column chromatography and Superdex 200 pg gel filtration

Ni-NTA agarose column chromatography and Superdex 200 pg gel filtration

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Ni-NTA column chromatography and Superdex 200 gel filtration

Ni-NTA resin column chromatography and Superdex 200 gel filtration

nickel Sepharose column chromatography and ENrich SEC 650 gel filtration

A0R723

740023

recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

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668574

recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) solubilized from inclusion bodies and refolded is further purified by nickel affinity chromatography

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recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography

recombinant His10-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration

recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

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recombinant protein

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recombinant protein, modified purification protocol

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684702

using Ni-NTA chromatography

wild-type and mutants purified to homogeneity using an Ni2+-nitrilotriacetic acid affinity column

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763622

C-terminal His-tagged FabG from Staphylococcus aureus is cloned into the NcoI and XhoI cloning sites of the vector pET28a, expressed in BL21 DE3 Escherichia coli

Staphylococcus aureus

Q2FZ53

coexpression in Escherichia coli LS5218 with fabH mutant F87T and polyhydroxyalkanoate synthase genes

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685775

complementation of Escherichia coli fabG mutant with Lactobacillus lactis fabG genes shows that fabG1 encodes a functional beta-ketoacyl ACP reductase and fabG2 encodes an enzyme that has activity with the model substrate beta-ketobutyryl-CoA, but lacks the ability to support fatty acid synthesis both in vivo and in vitro

Lactococcus lactis

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654725

expressed in Escherichia coli

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expressed in Escherichia coli as a His-tagged fusion protein

expressed in Escherichia coli BL21 (RARE) cells

expressed in Escherichia coli BL21 Rosetta 2 (DE3) pLysS cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells and in Corynebacterium glutamicum

expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells

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expression in Escherichia coli

5 entries

expression in Saccharomyces cerevisae mutant cells lacking the homologous mitochondrial FASII enzyme 3-oxoacyl-ACP reductase Oar1p

Caenorhabditis elegans

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704721

expression in Streptomyces cerevisiae cells lacking 3-oxoacyl-ACP reductase

P9WGT3, O53665

expression of protein without transit peptide in Escherichia coli

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FabG1 expressed from vector pPLM189 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG1 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production

P9WGT3, O53665

FabG4 expressed from vector pPLM192 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG4 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production

P9WGT3, O53665

gene fabG, DNA and amino acid sequence determination and analysis, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)

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668574

gene fabG, DNA and amino acid sequence determination and analysis, expression of His10-tagged enzyme in Escherichia coli

gene fabG, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)

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gene fabG, overexpression of His-tagged enzyme in strain BL21(DE3)

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667257

gene fabG, overexpression of His-tagged enzyme in strain BL21(DE3), recombinant expression in Escherichia coli strain JM109 leads to enhanced production of polyhydroxyalkanoate, PHA, copolymer from glucose, PHA composition, overview

Pseudomonas sp.

Q4AE87

667257

gene rhlG, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) or, as selenomethionine-labeled variant in Escherichia coli strain B834 in minimal medium

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heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with fabG1 in Haloferax volcanii

Haloarcula hispanica

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701808

heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with Haloarcula hispanica fabG1 reconstructs the polyhydroxyalkanoate biosynthetic pathway

Haloferax volcanii

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701808

His-tagged FabG expressed in Escherichia coli strain BL21 (DE3)

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into pET-28a vector and expressed in Escherichia coli BL21 (DE3) codon plus

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706639

N-terminal 6 × His-tagged Xcc FabG3 recombinant protein is expressed in Escherichia coli BL21 (DE3)

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763477

N-terminal His-tagged FabG from Escherichia coli is cloned into the NcoI and XhoI cloning sites of the vector pET28a, expressed in BL21 DE3 Escherichia coli

NH2-terminally His-tagged FabG expressed in Escherichia coli strain BL21(DE3)

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overexpressed in Escherichia coli BL21 (DE3)

synthetic construct

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overexpression in Escherichia coli strain BL21 (DE3)

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285682

overexpression of fabG gene in Escherichia coli strain BL21 (DE3)

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285681

overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies

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PCR product recombined with pDONR221 and insert from this vector transferred in the LR reaction to the expression vector pET15g which adds a histidine tag and a 3C protease cleavage site, expressed in Escherichia coli B834(DE3) cells

Bacillus anthracis

Q81JG6

706640

pET15b-fabG vector construct transformed into the Escherichia coli BL21 DE3 strain

Recombinant Escherichia coli (strain DH5alpha) co-expresses the fabG gene. The fabG gene is PCR-cloned using primers derived from the up and down-stream regions of the Pseudomonas putida KT2440 genome.

Pseudomonas putida

A5HIF6

693287

recombinant hexahistidine-tagged FabG2 is expressed in Escherichia coli

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selection of an Escherichia coli, BL21(DE3)NH host that stably expresses mutant forms of 3-ketoacyl-ACP(CoA) reductase

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657270

transformation of the fabG gene encoding 3-ketoacyl-[acyl-carrier-protein] reductase in fusion with a His6-MBP-tag (ligated into vector pETM-41) into Escherichia coli XL-10 Gold. After isolation from XL-10 cells and DNA sequencing, transformed into Escherichia coli Tuner (DE3) cells

transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter

Q949M3

689500

wild-type and mutants cloned into the pET-28a(+) vector and expressed in Escherichia coli BL21 (DE3) codon plus

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YFP-KCR1 and CFP-KCR2 fusion constructs transiently expressed in tobacco under the control of the 35S promoter or in Arabidopsis. KCR1 and KCR2 expressed in the yeast ybr159DELTA mutant

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700827

elevated expression detected after tachyplesin III treatment

solubilization of overexpressed recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) inclusion bodies by 8 M urea, and refolding by dialysis, cation exchange chromatography, and dilution in presence of 0.001 mM NADPH in 20 mM sodium acetate, pH 5.3, 10% glycerol, and 0.05% Tween 20, the refolded enzyme shows 90-95% of soluble enzyme activity

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study on guanidinium chloride-induced isothermal and thermal denaturation. Folding/unfolding is completely reversible and a two-state process. Conformational stability, i.e. DELTAGS, and the DELTACP value for the protein unfolding, are 22.68 kcal/mole and 5.83 kcal/(mole K)

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687216

drug development

30 entries

synthesis