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Literature summary extracted from

  • Sawhney, S.K.; Nicholas, D.J.D.
    Nitrite, hydroxylamine and sulphite reductases in wheat leaves (1975), Phytochemistry, 14, 1499-1503.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.99.1 chloroplast
-
Triticum aestivum 9507
-

Organism

EC Number Organism UniProt Comment Textmining
1.7.99.1 Triticum aestivum
-
wheat, nitrite reductase and hydroxylamine reductase are distinct enzymes
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.7.99.1 leaf
-
Triticum aestivum
-

Storage Stability

EC Number Storage Stability Organism
1.7.99.1 0°C, 65% activity with methyl viologen after 24 hours, 40% activity with benzyl viologen after 24 hours Triticum aestivum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.99.1 hydroxylamine + reduced acceptor methyl viologen is more effective than benzyl viologen, flavin nucleotides are also utilized but to a lesser extent Triticum aestivum ammonia + oxidized acceptor
-
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Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.7.99.1 45
-
20 min, 25-38% loss of activity Triticum aestivum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.99.1 7.8
-
-
Triticum aestivum