Abstract
A glycolate dehydrogenase found in the marine diatom Thallassiosira pseudonana differs significantly from that occurring in other algal systems. It is insensitive to cyanide and prefers the l-isomer of lactic acid although the d-isomer is oxidized slowly. Its specific activity is comparatively high; substrate affinity is rather low (glycolate K m 1.6×10-2 and l(+)lactate K m 2.2×10-2); optimal activity occurs at pH 8.7. It appears to be indirectly linked to oxygen via a system of electron carriers; it is insensitive to metal complexing agents but is partially inactivated by sulfhydryl inhibitors. Attempts to identify possible cofactors were unsuccessful.
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Paul, J.S., Volcani, B.E. Photorespiration in diatoms. Arch. Microbiol. 101, 115–120 (1974). https://doi.org/10.1007/BF00455931
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DOI: https://doi.org/10.1007/BF00455931