Cyanide formation from glyoxylate and hydroxylamine catalysed by extracts of higher-plant leaves

Extracts of spinach, maize and barley contain an enzyme which catalyses the formation of hydrogen cyanide from glyoxylate and hydroxylamine. The enzyme is dependent upon ADP and a divalent cation such as manganese. Glyoxylic-acid oxime is a poor substrate for the enzyme. Carbon dioxide is another pr...

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Bibliographic Details
Published in:Planta 1982, Vol.156 (6), p.487-491
Main Authors: Hucklesby, D.P, Dowling, M.J, Hewitt, E.J
Format: Article
Language:English
Subjects:
Barley
corn
Cyanides
Enzyme substrates
Enzymes
Glyoxylates
Hordeum vulgare
Hydrogen
Nitrates
Nitrites
Oximes
Spinach
Spinacia oleracea
Zea mays
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Summary:Extracts of spinach, maize and barley contain an enzyme which catalyses the formation of hydrogen cyanide from glyoxylate and hydroxylamine. The enzyme is dependent upon ADP and a divalent cation such as manganese. Glyoxylic-acid oxime is a poor substrate for the enzyme. Carbon dioxide is another product of the reaction and is probably produced in 1:1 stoichiometry with hydrogen cyanide. The possible relationship of this enzyme to the regulation of nitrate reduction is discussed.
ISSN:0032-0935
1432-2048
DOI:10.1007/BF00392769