1.8.1.14: CoA-disulfide reductase

This is an abbreviated version!
For detailed information about CoA-disulfide reductase, go to the full flat file.

Reaction

2 CoA +

Synonyms

BACoADR, BB0728, CoA disulfide reductase, CoA-disulfide reductase (NADH), CoA-disulfide reductase (NADH2), CoADR, coenzyme A disulfide reductase, coenzyme A disulphide reductase, coenzyme A-disulfide reductase, EC 1.6.4.10, NADH-dependent coenzyme A disulfide reductase, NADH2:CoA-disulfide oxidoreductase, NADH:CoA-disulfide oxidoreductase, PH0572

ECTree

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.1 With NAD⁺ or NADP⁺ as acceptor

                1.8.1.14 CoA-disulfide reductase

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Results	in table
1995	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
37	Cofactor
8	Crystallization (Commentary)
5	General Information
7	Inhibitors
8	kcat/KM [mM/s]
7	Ki Value [mM]
27	KM Value [mM]
2	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
25	Organism
2	Pathway
27	PDB ID
1	pH Optimum
12	Protein Variants
10	Purification (Commentary)
2	Reaction
3	Reaction Type
23	Reference
2	Source Tissue
4	Specific Activity [micromol/min/mg]
42	Substrates and Products (Substrate)
8	Subunits
48	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
35	Turnover Number [1/s]

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Reference on EC 1.8.1.14 - CoA-disulfide reductase

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

394071

Setlow, B.; Setlow, P.

Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant germinated spores and growing and sporulating cells of Bacillus megaterium

J. Bacteriol.

132

444-452

1979

Priestia megaterium, Priestia megaterium QM

410791

brenda

655529

Harris, D.R.; Ward, D.E.; Feasel, J.M.; Lancaster, K.M.; Murphy, R.D.; Mallet, T.C.; Crane, E.J., 3rd

Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles

FEBS J.

272

1189-1200

2005

Pyrococcus horikoshii

15720393

brenda

672062

Mallett, T.C.; Wallen, J.R.; Karplus, P.A.; Sakai, H.; Tsukihara, T.; Claiborne, A.

Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution

Biochemistry

45

11278-11289

2006

Staphylococcus aureus (O52582), Staphylococcus aureus

16981688

brenda

673721

Hummel, C.S.; Lancaster, K.M.; Crane, E.J.

Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: implications for a general role for coenzyme A in thermophiles

FEMS Microbiol. Lett.

252

229-234

2005

Pyrococcus furiosus, Saccharolobus solfataricus, Thermococcus litoralis

16213671

brenda

676059

Boylan, J.A.; Hummel, C.S.; Benoit, S.; Garcia-Lara, J.; Treglown-Downey, J.; Crane, E.J.; Gherardini, F.C.

Borrelia burgdorferi bb0728 encodes a coenzyme A disulphide reductase whose function suggests a role in intracellular redox and the oxidative stress response

Mol. Microbiol.

59

475-486

2006

Borreliella burgdorferi, Borreliella burgdorferi bb0728

16390443

brenda

685242

Wallen, J.R.; Paige, C.; Mallett, T.C.; Karplus, P.A.; Claiborne, A.

Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity

Biochemistry

47

5182-5193

2008

Bacillus anthracis

18399646

brenda

685514

Revell, K.D.; Heldreth, B.; Long, T.E.; Jang, S.; Turos, E.

N-Thiolated beta-lactams: Studies on the mode of action and identification of a primary cellular target in Staphylococcus aureus

Bioorg. Med. Chem.

15

2453-2467

2007

Staphylococcus aureus

17258460

brenda

712246

van der Westhuyzen, R.; Strauss, E.

Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus

J. Am. Chem. Soc.

132

12853-12855

2010

Staphylococcus aureus

20738089

brenda

712964

Case, C.L.; Rodriguez, J.R.; Mukhopadhyay, B.

Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii

Microbiology

155

69-79

2009

no activity in Methanocaldococcus jannaschii

19118348

brenda

724355

Wallace, B.D.; Edwards, J.S.; Wallen, J.R.; Moolman, W.J.; van der Westhuyzen, R.; Strauss, E.; Redinbo, M.R.; Claiborne, A.

Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights

Biochemistry

51

7699-7711

2012

Staphylococcus aureus (Q2FIA5), Staphylococcus aureus

22954034

brenda

724377

Herwald, S.; Liu, A.Y.; Zhu, B.E.; Sea, K.W.; Lopez, K.M.; Sazinsky, M.H.; Crane, E.J.

Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr): implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus

Biochemistry

52

2764-2773

2013

Pyrococcus horikoshii (O58308), Pyrococcus horikoshii

23530771

brenda

726003

Eggers, C.H.; Caimano, M.J.; Malizia, R.A.; Kariu, T.; Cusack, B.; Desrosiers, D.C.; Hazlett, K.R.; Claiborne, A.; Pal, U.; Radolf, J.D.

The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian host

Mol. Microbiol.

82

679-697

2011

Borreliella burgdorferi, Borreliella burgdorferi B31

21923763

brenda

744312

Herwald, S.; Liu, A.; Zhu, B.; Sea, K.; Lopez, K.; Sazinsky, M.; Crane, E.

Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr). Implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus

Biochemistry

52

2764-2773

2013

Pyrococcus horikoshii (O58308), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58308)

23530771

brenda

764212

Lencina, A.M.; Koepke, J.; Preu, J.; Muenke, C.; Gennis, R.B.; Michel, H.; Schurig-Briccio, L.A.

Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus

Biochim. Biophys. Acta Bioenerg.

1860

148080

2019

Thermus thermophilus (Q72HK3), Thermus thermophilus, Thermus thermophilus ATCC BAA-163 (Q72HK3)

31520616

brenda

764676

Sea, K.; Lee, J.; To, D.; Chen, B.; Sazinsky, M.H.; Crane, E.J.

A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry

FEBS open bio

8

1083-1092

2018

Pyrococcus horikoshii (O58308), Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860 (O58308)

29988575

brenda

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