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Ligand trans-2,3-dehydroacyl-[acyl-carrier protein]

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for trans-2,3-dehydroacyl-[acyl-carrier protein]

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH = acyl-[acyl-carrier protein] + NADP+

656515

-

1.3.1.9

a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+ = an acyl-[acyl-carrier protein] + NAD+

741435, 740920, 765104

-

1.3.1.9

a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ = an acyl-[acyl-carrier protein] + NADP+

765104

-

1.3.1.9

enoyl esters of acyl-carrier protein + NADH = ?

390875, 390888, 390874

-

1.3.1.9

trans-2-enoyl-acyl-ACP + NADH + H+ = acyl-ACP + NAD+

697740

-

1.3.1.9

4 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

0

-

1.3.1.9

an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+

0

-

1.3.1.9

acyl-[acyl-carrier protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+

0

-

1.3.1.9

2 entries

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ = acyl-[acyl-carrier protein] + NADP+

685233

-

1.3.1.10

trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH = acyl-[acyl-carrier protein] + NADP+

656515

-

1.3.1.9

a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+ = an acyl-[acyl-carrier protein] + NAD+

741435, 740920, 765104

-

1.3.1.9

a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ = an acyl-[acyl-carrier protein] + NADP+

765104

-

1.3.1.9

enoyl esters of acyl-carrier protein + NADH = ?

390875, 390888, 390874

-

1.3.1.9

trans-2-enoyl-ACP + NADH + H+ = acyl-ACP + NAD+

689328

-

1.3.1.9

trans-2-enoyl-acyl-ACP + NADH + H+ = acyl-ACP + NAD+

697740

-

1.3.1.10

2 entries

1.3.1.9

5 entries

Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

0

-

1.3.1.10

acyl-[acyl-carrier protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

0

-

1.3.1.9

an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+

0

-

1.3.1.9

acyl-[acyl-carrier protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH

0

-

1.3.1.9

acyl-[acyl-carrier protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+

0

-

1.3.1.10

2 entries

1.3.1.9

3 entries

Enzyme Kinetic Parameters

References & Links

Literature References (10)

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Show Reference (10 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

390874

2194572

Immunological detection of NADH-specific enoyl-ACP reductase from rape seed (Brassica napus)-induction, relationship of alpha and beta polypeptides, mRNA translation and interaction with ACP

1990

Slabas, A.R.; Cottingham, I.R.; Austin, A.; Hellyer, A.; Safford, R.; Smith, C.G.

Biochim. Biophys. Acta

1039

181-188

390875

2706276

Inhibition and covalent modification of rape seed (Brassica napus) enoyl ACP reductase by phenylglyoxal

1989

Cottingham, I.R.; Austin, A.J.; Slabas, A.R.

Biochim. Biophys. Acta

995

273-278

390888

9878369

The x-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 ANG resolution

1998

Baldock, C.; Rafferty, J.B.; Stuitje, A.R.; Slabas, A.R.; Rice, D.W.

J. Mol. Biol.

284

1529-1546

656515

12614607

Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance

2003

Airenne, T.T.; Torkko, J.M.; Van den plas, S.; Sormunen, R.T.; Kastaniotis, A.J.; Wierenga, R.K.; Kalervo Hiltunen, J.

J. Mol. Biol.

327

47-59

685233

18335995

Mechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureus

2008

Xu, H.; Sullivan, T.J.; Sekiguchi, J.; Kirikae, T.; Ojima, I.; Stratton, C.F.; Mao, W.; Rock, F.L.; Alley, M.R.; Johnson, F.; Walker, S.G.; Tonge, P.J.

Biochemistry

47

4228-4236

689328

17697396

Type I and type II fatty acid biosynthesis in Eimeria tenella: enoyl reductase activity and structure

2007

Lu, J.Z.; Muench, S.P.; Allary, M.; Campbell, S.; Roberts, C.W.; Mui, E.; McLeod, R.L.; Rice, D.W.; Prigge, S.T.

Parasitology

134

1949-1962

697740

19217192

Design and in silico screening of combinatorial library of antimalarial analogs of triclosan inhibiting Plasmodium falciparum enoyl-acyl carrier protein reductase

2009

Frecer, V.; Megnassan, E.; Miertus, S.

Eur. J. Med. Chem.

44

3009-3019

740920

25891098

Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach

2015

Chollet, A.; Mourey, L.; Lherbet, C.; Delbot, A.; Julien, S.; Baltas, M.; Bernadou, J.; Pratviel, G.; Maveyraud, L.; Bernardes-Genisson, V.

J. Struct. Biol.

190

328-337

741435

28436453

Functional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme

2017

Martinelli, L.K.B.; Rotta, M.; Villela, A.D.; Rodrigues-Junior, V.S.; Abbadi, B.L.; Trindade, R.V.; Petersen, G.O.; Danesi, G.M.; Nery, L.R.; Pauli, I.; Campos, M.M.; Bonan, C.D.; de Souza, O.N.; Basso, L.A.; Santos, D.S.

Sci. Rep.

7

46696

765104

32762412

In vitro and in silico analysis of L. donovani enoyl acyl carrier protein reductase - A possible drug target

2021

Yadav, S.; Mandal, H.; Saravanan, V.; Das, P.; Singh, S.

J. Biomol. Struct. Dyn.

39

6056-6069

Links to other databases for trans-2,3-dehydroacyl-[acyl-carrier protein]

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