The active sites of metalloenzymes that catalyze O 2-dependent reactions generally contain
iron or copper ions. However, several enzymes are capable of activating O 2 at manganese …

Remarkably few enzymes are known to employ a mononuclear manganese ion that
undergoes changes in redox state during catalysis. Many questions remain to be answered …

The ethylene-forming enzyme (EFE) from Pseudomonas syringae pv. phaseolicola PK2 is a
member of the mononuclear nonheme Fe (II)-and 2-oxoglutarate (2OG)-dependent …

Ethylene-forming enzyme (EFE) is an ambifunctional iron (II)-and 2-oxoglutarate-dependent
(Fe/2OG) oxygenase. In its major (EF) reaction, it converts carbons 1, 2, and 5 of 2OG to …

Acireductone dioxygenase (ARD) from the methionine salvage pathway (MSP) is a unique
enzyme that exhibits dual chemistry determined solely by the identity of the divalent …

Although it is a member of the amidohydrolase superfamily, LigW catalyzes the nonoxidative
decarboxylation of 5-carboxyvanillate to form vanillate in the metabolic pathway for bacterial …

Campylobacter jejuni is a Gram-negative, pathogenic bacterium that causes
campylobacteriosis, a form of gastroenteritis. C. jejuni is the most frequent cause of food …

Oxalate decarboxylase (OXDC) is a typical Mn2+/Mn3+ dependent metal enzyme and splits
oxalate to formate and CO2 without any organic cofactors. Fungi and bacteria are the main …

The enzyme ForT catalyzes C–C bond formation between 5′-phosphoribosyl-1′-
pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3, 5-dicarboxylate to make a key …

The hexameric low-pH stress response enzyme oxalate decarboxylase catalyzes the
decarboxylation of the oxalate mono-anion in the soil bacterium Bacillus subtilis. A single …