Detection and Characterization of Sorbitol Dehydrogenase from Apple Callus Tissue 12
AUTOR(ES)
Negm, Fayek B.
RESUMO
Sorbitol dehydrogenase (l-iditol:NAD+ oxidoreductase, EC 1.1.1.14) has been detected and characterized from apple (Malus domestica cv. Granny Smith) mesocarp tissue cultures. The enzyme oxidized sorbitol, xylitol, l-arabitol, ribitol, and l-threitol in the presence of NAD. NADP could not replace NAD. Mannitol was slightly oxidized (8% of sorbitol). Other polyols that did not serve as substrate were galactitol, myo-inositol, d-arabitol, erythritol, and glycerol. The dehydrogenase oxidized NADH in the presence of d-fructose or l-sorbose. No detectable activity was observed with d-tagatose. NADPH could partially substitute for NADH.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=543026Documentos Relacionados
- Factors Affecting Growth of Tobacco Callus Tissue and Its Incorporation of Tyrosine 12
- Caracterização do gene que codifica a enzima sorbitol desidrogenase em milho
- Sorbitol-6-Phosphate Dehydrogenase from Loquat Fruit 1
- Purification and Characteristics of Sorbitol-6-phosphate Dehydrogenase from Loquat Leaves 1
- d-SORBITOL-6-PHOSPHATE DEHYDROGENASE FROM LACTOBACILLUS CASEI1
