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Literature summary for 1.8.1.8 extracted from

  • Lessner, D.J.; Ferry, J.G.
    The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster (2007), J. Bacteriol., 189, 7475-7484.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.8

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Methanosarcina acetivorans

Metals/Ions

Metals/Ions Comment Organism Structure
Iron-sulfur cluster the enzyme contains an intermolecular Fe-S cluster that controls oligomerization as a mechanism to regulate protein disulfide reductase activity Methanosarcina acetivorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein disulfide + NADH Methanosarcina acetivorans the activity of MdrA and the organization of mdrA in a transcriptional unit with oxidative stress genes are consistent with a role in the oxidative stress response of Methanosarcina acetivorans protein dithiol + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina acetivorans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein disulfide + NADH
-
 Methanosarcina acetivorans protein dithiol + NAD+
-
 ?
protein disulfide + NADH the activity of MdrA and the organization of mdrA in a transcriptional unit with oxidative stress genes are consistent with a role in the oxidative stress response of Methanosarcina acetivorans Methanosarcina acetivorans protein dithiol + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
MA3736
-
 Methanosarcina acetivorans
MdrA
-
 Methanosarcina acetivorans

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Methanosarcina acetivorans