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Ligand (3S)-citryl-CoA

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for (3S)-citryl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.34

(3S)-citryl-CoA = acetyl-CoA + oxaloacetate

747993, 653277

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In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.8.3.10

acetyl-CoA + citrate = acetate + (3S)-citryl-CoA

643831

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6.2.1.18

ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA

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Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.34

(3S)-citryl-CoA = acetyl-CoA + oxaloacetate

33348, 33347, 653277, 673369, 747993

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Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.8.3.10

acetyl-CoA + citrate = acetate + (3S)-citryl-CoA

643831

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2.8.3.10

butyryl-CoA + citrate = butyrate + (3S)-citryl-CoA

643831

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2.8.3.10

propionyl-CoA + citrate = propionate + (3S)-citryl-CoA

643831

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6.2.1.18

ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA

661,

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6.2.1.18

ATP + citrate + CoA = ADP + phosphate + citryl-CoA

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-

2.8.3.10

3 entries

6.2.1.18

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (4 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (4 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.3.8

6z2h, 3D-view

2.3.3.8

6znw, 3D-view

2.3.3.8

6z2h, 3D-view

2.3.3.8

6znw, 3D-view

2.3.3.8

4 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.8.3.10

26.7

-

pH 8.0, 25°C

643831

4.1.3.34

570

-

pH 8.0, 70°C

653277

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.8.3.10

0.2

-

pH 8.0, 25°C

643831

4.1.3.34

0.082

-

pH 8.0, 70°C

653277

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

661

6749502

Isolation of enzymically active fragments formed by limited proteolysis

1982

Lill, U.; Schreil, A.; Eggerer, H.

Eur. J. Biochem.

125

645-650

33347

2205500

Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit

1990

Hupperich, M.; Henschen, A.; Eggerer, H.

Eur. J. Biochem.

192

161-166

33348

1684105

Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid

1991

Man, W.J.; Li, Y.; O'Connor, C.D.; Wilton, D.C.

Biochem. J.

280

521-526

643831

336371

Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate

1977

Dimroth, P.; Loyal, R.; Eggerer, H.

Eur. J. Biochem.

80

479-488

653277

15101982

A novel enzyme, citryl-CoA lyase, catalysing the second step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6

2004

Aoshima, M.; Ishii, M.; Igarashi, Y.

Mol. Microbiol.

52

763-770

673369

17227414

Autotrophic CO2 fixation via the reductive tricarboxylic acid cycle in different lineages within the phylum Aquificae: Evidence for two ways of citrate cleavage

2007

Hugler, M.; Huber, H.; Molyneaux, S.J.; Vetriani, C.; Sievert, S.M.

Environ. Microbiol.

9

81-92

747993

26418853

A phylogenetic approach to the early evolution of autotrophy the case of the reverse TCA and the reductive acetyl-CoA pathways

2014

Becerra, A.; Rivas, M.; Garcia-Ferris, C.; Lazcano, A.; Pereto, J.

Int. Microbiol.

17

91-97

Links to other databases for (3S)-citryl-CoA

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Show Links (1 entry)

ChEBI

PubChem

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