Answers are grounded in this paper and cite their sources.
A new enzyme was partially purified from D. melanogaster. The enzyme catalyzes the reduction of xanthommatin to dihydroxanthommatin in the presence of NADH/H+ as confactor. FAD, FMN, p‐chloromercuribenzoate, 2‐amino‐4‐hydroxypteridine and biopterin inhibited the enzyme activity. The inhibitory effect of some pterines suggests a correlation between the synthesis of dihydroxanthommatin and that of pterines. It has been suggested that the enzyme may participate, in vivo, in the reduction of xanthommatin.
No takes yet. Share an insight, caveat, or question.
Santoro et al. (1986) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: