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Literature summary extracted from

  • Bagnaresi, P.; Mazars-Marty, D.; Pupilld, P.; Marty, F.; Briat, J.F.
    Tonoplast subcellular localization of maize cytochrome b5 reductases (2000), Plant J., 24, 645-654.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 expression in Saccharomaces cerevisiae Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 tonoplast
-
 Zea mays
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH Zea mays enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Zea mays Q8W2K4
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 root
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals Zea mays 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome c + NADH isoforms I and II, 16% and 27% of Fe3+-citrate reduction respectively Zea mays 2 ferrocytochrome c + NAD+ + H+
-
 ?
1.6.2.2 Cu2+-citrate + NADH isoforms I and II, 59 and 47% of Fe3+-citrate reduction respectively Zea mays Cu+-citrate + NAD+
-
 ?
1.6.2.2 Fe3+-citrate + NADH isoforms I and II Zea mays Fe2+-citrate + NAD+
-
 ?
1.6.2.2 Fe3+-EDTA + NADH isoforms I and II Zea mays Fe2+-EDTA + NAD+
-
 ?