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Ligand 4-hydroxybenzoyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

phenol degradation

KEGG

Aminobenzoate degradation, Benzoate degradation, Biosynthesis of secondary metabolites, Degradation of aromatic compounds, Fluorobenzoate degradation, Microbial metabolism in diverse environments, Ubiquinone and other terpenoid-quinone biosynthesis more

MetaCyc

4-chlorobenzoate degradation, 4-coumarate degradation (anaerobic), 4-ethylphenol degradation (anaerobic), 4-hydroxybenzoate biosynthesis III (plants), phenol degradation II (anaerobic)

Show all BRENDA pathways known for 4-hydroxybenzoyl-CoA

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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

1.1.7.1

4-hydroxybenzoyl-CoA + reduced electron donor = benzoyl-CoA + oxidized electron donor + H2O

756636

-

3.1.2.20

4-Hydroxybenzoyl-CoA + H2O = 4-Hydroxybenzoate + CoA

690932

-

3.1.2.23

4-Hydroxybenzoyl-CoA + H2O = 4-Hydroxybenzoate + CoA

650103, 690642, 652279, 652473

1lo9, 3D-view

3.1.2.23

4-Hydroxybenzoyl-CoA + H2O = ?

23921

1lo9, 3D-view

3.1.2.23

2 entries

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

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.7.1

benzoyl-CoA + oxidized electron donor + H2O = 4-hydroxybenzoyl-CoA + reduced electron donor

-

-

1.1.7.1

benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin

-

-

1.1.7.1

2 entries

3.8.1.7

4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride

-

-

6.2.1.27

ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA

, 648907, 648909, 288500

-

Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Substrate (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.7.1

4-hydroxybenzoyl-CoA + acceptor = benzoyl-CoA + reduced acceptor

288503, 288499, 288502, 288504, 288500, 288501, 657371, 288505, 672322, 672474

-

1.1.7.1

4-hydroxybenzoyl-CoA + reduced electron donor = benzoyl-CoA + oxidized electron donor + H2O

756636

-

1.1.7.1

2 entries

1.3.7.8

4-hydroxybenzoyl-CoA + reduced methyl viologen + ATP = 4-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized methyl viologen + ADP + phosphate

12559

-

2.3.1.151

4-hydroxybenzoyl-CoA + 3 malonyl-CoA = 2,4,4',6-trihydroxybenzophenone + 4 CoA + 3 CO2

660170

-

2.3.1.151

Malonyl-CoA + 4-hydroxybenzoyl-CoA = ?

16327

-

2.3.1.151

2 entries

2.3.1.302

4-hydroxybenzoyl-CoA + 5-hydroxyanthranilate = an avenanthramide + CoA

762520

-

3.1.2.20

4-Hydroxybenzoyl-CoA + H2O = 4-Hydroxybenzoate + CoA

690932

-

3.1.2.20

4-hydroxybenzoyl-CoA + H2O = CoA + 4-hydroxybenzoate

696310

-

3.1.2.23

4-Hydroxybenzoyl-CoA + H2O = 4-Hydroxybenzoate + CoA

780, 781, 23921, 650103, 652279, 652473, 678580, 690642, 729220, 707108

1lo9, 3D-view

3.1.2.23

4-Hydroxybenzoyl-CoA + H2O = ?

23921

1lo9, 3D-view

3.1.2.20

2 entries

3.1.2.23

2 entries

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.7.1

benzoyl-CoA + oxidized electron donor + H2O = 4-hydroxybenzoyl-CoA + reduced electron donor

-

-

1.1.7.1

benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin

-

-

3.8.1.7

4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride

-

-

3.8.1.7

4-bromobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + bromide

-

-

3.8.1.7

4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride

, 33077

-

3.8.1.7

4-fluorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + fluoride

-

-

3.8.1.7

4-iodobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + iodide

-

-

1.1.7.1

2 entries

3.8.1.7

5 entries

6.2.1.25

ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA

651721, , 649526

-

6.2.1.27

ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA

, 648909, 648907, 288500

-

6.2.1.27

CTP + 4-hydroxybenzoate + CoA = CMP + 4-hydroxybenzoyl-CoA + diphosphate

-

-

6.2.1.27

2 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.8.1.7

competitive

654589

-

3D Structure of Enzyme-Ligand-Complex (PDB) (5 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (5 entries)

EC NUMBER

ENZYME 3D STRUCTURE

3.1.2.23

1lo9, 3D-view

3.8.1.6

1jxz, 3D-view

3.8.1.6

1nzy, 3D-view

3.8.1.6

1jxz, 3D-view

3.8.1.6

1nzy, 3D-view

3.8.1.6

4 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (37 results)

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Show Turnover Number (37 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.2.20

0.0062

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.078

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.207

-

wild-type, at room temperature

696310

3.1.2.23

0.0001

-

mutant E73A, pH 7.5, 25°C

729220

3.1.2.23

0.00055

-

mutant D17N, pH 7.5, 25°C

650103

3.1.2.23

0.00084

-

mutant D17S, pH 7.5, 25°C

650103

3.1.2.23

0.0017

-

mutant E73Q, pH 7.5, 25°C

729220

3.1.2.23

0.0103

-

mutant T77D, pH 7.5, 25°C

729220

3.1.2.23

0.0417

-

mutant D31A, pH 7.5, 25°C

729220

3.1.2.23

0.11

-

mutant R126L, pH 7.5, 25°C

650103

3.1.2.23

0.123

-

mutant E73D, pH 7.5, 25°C

729220

3.1.2.23

0.127

-

mutant Q58A, pH 7.5, 25°C

729220

3.1.2.23

0.129

-

mutant E73D/T77S, pH 7.5, 25°C

729220

3.1.2.23

0.13

-

mutant Q58D, pH 7.5, 25°C

729220

3.1.2.23

0.13

-

mutant R88A, pH 7.5, 25°C

650103

3.1.2.23

0.14

-

mutant K90A, pH 7.5, 25°C

650103

3.1.2.23

0.15

-

mutant H64A, pH 7.5, 25°C

729220

3.1.2.23

0.15

-

mutant R128A, pH 7.5, 25°C

650103

3.1.2.23

0.17

-

mutant T77V, pH 7.5, 25°C

729220

3.1.2.23

0.18

-

wild-type enzyme and mutant R89L, pH 7.5, 25°C

650103

3.1.2.23

0.28

-

mutant H64Q, pH 7.5, 25°C

729220

3.1.2.23

0.364

-

mutant Q58E, pH 7.5, 25°C

729220

3.1.2.23

0.48

-

mutant D17E, pH 7.5, 25°C

650103

3.1.2.23

1.08

-

mutant E78A, pH 7.5, 25°C

729220

3.1.2.23

1.15

-

mutant D31N, pH 7.5, 25°C

729220

3.1.2.23

1.54

-

mutant E73D/T77A, pH 7.5, 25°C

729220

3.1.2.23

2.09

-

mutant T77A, pH 7.5, 25°C

729220

3.1.2.23

2.4

-

wild-type, solvent D2O, pH 7.5, 25°C

729220

3.1.2.23

3.16

-

mutant T77S, pH 7.5, 25°C

729220

3.1.2.23

6.7

-

wild-type, pH 7.5, 25°C

729220

3.1.2.23

6.8

-

-

780

3.1.2.23

9.5

-

mutant R150A, pH 7.5, 25°C

729220

3.1.2.23

9.7

-

mutant T121A, pH 7.5, 25°C

729220

3.1.2.23

10

-

recombinant enzyme

690642

3.1.2.23

10.1

-

mutant S120A, pH 7.5, 25°C

729220

3.1.2.23

18.3

-

pH 7.5, 25°C

678580

3.1.2.23

99

-

mutant R102A, pH 7.5, 25°C

729220

3.1.2.20

3 entries

3.1.2.23

34 entries

K_M Value (35 results)

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Show KM Value (35 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.7.1

0.06

-

-

288504

2.3.1.302

0.052

-

pH 7, temperature not specified in the publication

762520

3.1.2.20

0.025

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.19

-

wild-type, at room temperature

696310

3.1.2.23

0.00014

-

mutant K90A, pH 7.5, 25°C

650103

3.1.2.23

0.00038

-

mutant T77D, pH 7.5, 25°C

729220

3.1.2.23

0.00077

-

mutant T77S, pH 7.5, 25°C

729220

3.1.2.23

0.0012

-

mutant T77A, pH 7.5, 25°C

729220

3.1.2.23

0.0012

-

wild-type, pH 7.5, 25°C

729220

3.1.2.23

0.0016

-

mutant Q58A, pH 7.5, 25°C

729220

3.1.2.23

0.0016

-

mutant S120A, pH 7.5, 25°C

729220

3.1.2.23

0.0024

-

mutant D17E, pH 7.5, 25°C

650103

3.1.2.23

0.004

-

mutant D31A, pH 7.5, 25°C

729220

3.1.2.23

0.004

-

mutant Q58E, pH 7.5, 25°C

729220

3.1.2.23

0.0045

-

-

780

3.1.2.23

0.0045

-

mutant R88A, pH 7.5, 25°C

650103

3.1.2.23

0.0046

-

mutant E73D/T77A, pH 7.5, 25°C

729220

3.1.2.23

0.005

-

mutant R126L, pH 7.5, 25°C

650103

3.1.2.23

0.0052

-

mutant R89L, pH 7.5, 25°C

650103

3.1.2.23

0.0055

-

mutant T77V, pH 7.5, 25°C

729220

3.1.2.23

0.006

-

pH 7.5, 25°C

678580

3.1.2.23

0.006

-

wild-type enzyme, pH 7.5, 25°C

650103

3.1.2.23

0.0061

-

mutant T121A, pH 7.5, 25°C

729220

3.1.2.23

0.007

-

recombinant enzyme

690642

3.1.2.23

0.0073

-

mutant R128A, pH 7.5, 25°C

650103

3.1.2.23

0.0128

-

mutant D31N, pH 7.5, 25°C

729220

3.1.2.23

0.013

-

mutant E73D/T77S, pH 7.5, 25°C

729220

3.1.2.23

0.014

-

mutant R102A, pH 7.5, 25°C

729220

3.1.2.23

0.0142

-

mutant E73Q, pH 7.5, 25°C

729220

3.1.2.23

0.015

-

mutant R150A, pH 7.5, 25°C

729220

3.1.2.23

0.018

-

mutant E73D, pH 7.5, 25°C

729220

3.1.2.23

0.096

-

mutant E78A, pH 7.5, 25°C

729220

3.1.2.23

0.18

-

mutant Q58D, pH 7.5, 25°C

729220

3.1.2.23

0.237

-

mutant H64Q, pH 7.5, 25°C

729220

3.1.2.23

0.51

-

mutant H64A, pH 7.5, 25°C

729220

3.1.2.20

2 entries

3.1.2.23

31 entries

K_i Value (8 results)

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Show KI Value (8 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.8.1.7

0.0017

-

mutant R257K, pH 7.5, 25°C

654589

3.8.1.7

0.0024

-

mutant R24K, pH 7.5, 25°C

654589

3.8.1.7

0.0025

-

wild-type enzyme, pH 7.5, 25°C

654589

3.8.1.7

0.0062

-

mutant R67K, pH 7.5, 25°C

654589

3.8.1.7

0.0165

-

mutant R24L, pH 7.5, 25°C

654589

3.8.1.7

0.019

-

mutant R257L, pH 7.5, 25°C

654589

3.8.1.7

0.04

-

mutant G113A, pH 7.5, 25°C

654589

3.8.1.7

0.05

0.1

mutant G114A, pH 7.5, 25°C

654589

3.8.1.7

8 entries

References & Links

Literature References (33)

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Show Reference (33 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

780

1610806

Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3

1992

Chang, K.H.; Liang, P.H.; Beck, W.; Scholten, J.D.; Dunaway-Mariano, D.

Biochemistry

31

5605-5610

781

7765837

On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway

1994

Dunaway-Mariano, D.; Babbitt, P.C.

Biodegradation

5

259-276

12559

8575453

Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172

1995

Boll, M.; Fuchs, G.

Eur. J. Biochem.

234

921-933

16327

9459298

Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum

1997

Schmidt, W.; Beerhues, L.

FEBS Lett.

420

143-146

23921

9837940

The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3

1998

Benning, M.M.; Wesenberg, G.; Liu, R.; Taylor, K.L.; Duinaway-Mariano, D.; Holden, H.M.

J. Biol. Chem.

273

33572-33579

33077

7918379

Purification and characterization of 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain 4-CB1

1994

Crooks, G.P.; Copley, S.D.

Biochemistry

33

11645-11649

288499

2753161

Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species

1989

Glockler, R.; Tschech, A.; Fuchs, G.

FEBS Lett.

251

237-240

288500

9683649

Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica

1998

Heider, J.; Boll, M.; Breese, K.; Breinig, S.; Ebenau-Jehle, C.; Feil, U.; Gad'on, N.; Laempe, D.; Leuthner, B.; Mohamed, M.E.S.; Schneider, S.; Burchhardt, G.; Fuchs, G.

Arch. Microbiol.

170

120-131

288501

9490068

4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins

1998

Breese, K.; Fuchs, G.

Eur. J. Biochem.

251

916-923

288502

8477729

Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species

1993

Brackmann, R.; Fuchs, G.

Eur. J. Biochem.

213

563-571

288503

9006014

4-Hydroxybenzoyl coenzyme A reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Rhodopseudomonas palustris and shares features with molybdenum-containing hydroxylases

1997

Gibson, J.; Dispensa, M.; Harwood, C.S.

J. Bacteriol.

179

634-642

288504

7547899

Hydroxybenzoyl-CoA reductase: coupling kinetics and electrochemistry to derive enzyme mechanisms

1995

El Kasmi, A.; Brachmann, R.; Fuchs, G.; Ragsdale, S.W.

Biochemistry

34

11668-11677

288505

-

Anaerobic degradation of 4-hydroxybenzoate: reductive dehydroxylation of 4-hydroxybenzoyl-CoA and ATP formation during 4-hydroxybenzoate decarboxylation by the phenol-metabolizing bacteria of a stable, strictly anaerobic consortium

1994

Gallert, C.; Winter, J.

Appl. Microbiol. Biotechnol.

42

408-414

648907

2914844

Involvement of coenzyme A thioesters in anaerobic metabolism of 4-hydroxybenzoate by Rhosopseudomonas palustris

1989

Merkel, S.M.; Eberhard, A.E.; Gibson, J.; Harwood, C.S.

J. Bacteriol.

171

1-7

648909

8477728

Enzymes of anarobic metabolism pf phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species

1993

Biegert, T.; Altenschmidt, U.; Eckerskorn, C.; Fuchs, G.

Eur. J. Biochem.

213

555-561

649526

12054436

Purification and characterization of benzoate:coenzyme A ligase from Clarkia breweri

2002

Beuerle, T.; Pichersky, E.

ARCH. BIOCHEM. BIOPHYS.

400

258-264

650103

12220180

Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site

2002

Zhuang, Z.; Song, F.; Zhang, W.; Taylor, K.; Archambault, A.; Dunaway-Mariano, D.; Dong, J.; Carey, P.R.

Biochemistry

41

11152-11160

651721

12897012

Benzoate-coenzyme A ligase from Thauera aromatica: an enzyme acting in anaerobic and aerobic pathways

2003

Schuhle, K.; Gescher, J.; Feil, U.; Paul, M.; Jahn, M.; Schagger, H.; Fuchs, G.

J. Bacteriol.

185

4920-4929

652279

11997398

X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase

2002

Thoden, J.B.; Holden, H.M.; Zhuang, Z.; Dunaway-Mariano, D.

J. Biol. Chem.

277

27468-27476

652473

12907670

The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU

2003

Thoden, J.B.; Zhuang, Z.; Dunaway-Mariano, D.; Holden, H.M.

J. Biol. Chem.

278

43709-43716

654589

11747444

Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis

2001

Luo, L.; Taylor, K.L.; Xiang, H.; Wei, Y.; Zhang, W.; Dunaway-Mariano, D.

Biochemistry

40

15684-15692

657371

15576037

Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow

2004

Unciuleac, M.; Warkentin, E.; Page, C.C.; Boll, M.; Ermler, U.

Structure

12

2249-2256

660170

12795704

Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases

2003

Liu, B.; Falkenstein-Paul, H.; Schmidt, W.; Beerhues, L.

Plant J.

34

847-855

672322

15721605

Key enzymes in the anaerobic aromatic metabolism catalysing Birch-like reductions

2005

Boll, M.

Biochim. Biophys. Acta

1707

34-50

672474

16218872

Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism

2005

Boll, M.; Schink, B.; Messerschmidt, A.; Kroneck, P.M.H.

Biol. Chem.

386

999-1006

678580

16962159

Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis

2007

Song, F.; Zhuang, Z.; Dunaway-Mariano, D.

Bioorg. Chem.

35

1-10

690642

18542924

Benzoyl-coenzyme A thioesterase of Azoarcus evansii: properties and function

2008

Ismail, W.

Arch. Microbiol.

190

451-460

690932

18247525

Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA

2008

Zhuang, Z.; Song, F.; Zhao, H.; Li, L.; Cao, J.; Eisenstein, E.; Herzberg, O.; Dunaway-Mariano, D.

Biochemistry

47

2789-2796

696310

19193103

Preferential hydrolysis of aberrant iIntermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues (dagger)

2009

Guo, Z.F.; Sun, Y.; Zheng, S.; Guo, Z.

Biochemistry

48

1712-1722

707108

19635449

Monitoring enzyme catalysis in the multimeric state: direct observation of Arthrobacter 4-hydroxybenzoyl-coenzyme A thioesterase catalytic complexes using time-resolved electrospray ionization mass spectrometry

2009

Li, Z.; Song, F.; Zhuang, Z.; Dunaway-Mariano, D.; Anderson, K.S.

Anal. Biochem.

394

209-216

729220

22873756

The catalytic mechanism of the hotdog-fold enzyme superfamily 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU

2012

Song, F.; Thoden, J.B.; Zhuang, Z.; Latham, J.; Trujillo, M.; Holden, H.M.; Dunaway-Mariano, D.

Biochemistry

51

7000-7016

756636

9057820

Anaerobic metabolism of aromatic compounds

1997

Heider, J.; Fuchs, G.

Eur. J. Biochem.

243

577-596

762520

-

Induction of hydroxycinnamoyl-CoA hydroxyanthranilate N-hydroxycinnamoyl-transferase (HHT) activity in oat leaves by victorin C

1997

Ishihara, A.; Matsukawa, T.; Miyagawa, H.; Ueno, T.; Iwamura, H.; Mayama, S.; Ishihara, A.; Matsukawa, T.; Miyagawa, H.; Iwamura, H.

Z. Naturforsch. C

52

756-760

Links to other databases for 4-hydroxybenzoyl-CoA

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ChEBI

PubChem

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