Nitric oxide reversibly inhibits Bacillus subtilis oxalate decarboxylase.
نویسندگان
چکیده
Membrane inlet mass spectrometry (MIMS) has been employed to assay the catalytic activity of oxalate decarboxylase (OxDC), allowing us to demonstrate that nitric oxide (NO) reversibly inhibits the enzyme under dioxygen-depleted conditions. X-band EPR measurements do not provide any direct evidence for the interaction of NO with either of the Mn(II) centers in OxDC raising the possibility that there is a separate dioxygen-binding pocket in the enzyme.
منابع مشابه
Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase.
Bacillus subtilis has been shown to express a cytosolic oxalate decarboxylase (EC 4.1.1.2). The enzyme was induced in acidic growth media, particularly at pH 5.0, but not by oxalate. The enzyme was purified, and N-terminal sequencing identified the protein to be encoded by yvrK. The role of the first oxalate decarboxylase to be identified in a prokaryote is discussed.
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عنوان ژورنال:
- Chemical communications
دوره 47 11 شماره
صفحات -
تاریخ انتشار 2011