AI Article Synopsis
- Nitric oxide (NO) has been proposed to regulate the process of ADP-ribosylation in cells, as shown through experiments using radiolabeled proteins and tissue samples.
- The previous hypothesis that NO stimulates an endogenous ADP-ribosyltransferase was challenged when replication in a controlled environment only with GAPDH revealed that NO leads to the entire NAD molecule binding to the enzyme instead of just ADP-ribosylation.
- This research indicates that NO modifies GAPDH by enhancing its chemical reactivity, possibly through the nitrosylation of a specific cysteine amino acid located in the enzyme's active site.
Article Abstract
Nitric oxide (NO) has been suggested to act as a regulator of endogenous intracellular ADP-ribosylation, based on radiolabelling of proteins in tissue homogenates incubated with [32P]NAD and NO. After the NO-stimulated modification was replicated in a defined system containing only the purified acceptor protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the hypothesis of NO-stimulation of an endogenous ADP-ribosyltransferase became moot. The NO-stimulated, NAD-dependent modification of GAPDH was recently characterized as covalent binding of the whole NAD molecule to the enzyme, not ADP-ribosylation. With this result, along with the knowledge that GAPDH is stoichiometrically S-nitrosylated, the role of NO in protein modification with NAD may be viewed as the conferring of an unexpected chemical reactivity upon GAPDH, possibly due to nitrosylation of a cysteine in the enzyme active site.
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