Peroxidases EC.1.11.X, AA2	Single electron oxidation without oxygen transfer: [S]H2 +H2O2 ⇔ [P] + 2H2O
Class II heme peroxidases (PODs) EC 1.11.1	Secreted by lignin depolymerizing WR fungi; enzymes share a conserved helical fold with 2 domains forming a heme-binding cleft.
Lignin Peroxidase (LiP) EC 1.11.1.14	High redox potential (RP) (1.4–1.5 V) of LiP facilitates oxidation of non-aromatic compounds without a mediator; LiP exhibit broad substrate specificity with (non)aromatic compounds and catalyze cleavage of the Cα-Cβ linkages of lignin polymers; Substrate oxidation occurs via long-range electron transfer to the heme from a hydroxylated Trp residue located on the protein surface.
Manganese Peroxidase (MnP) EC 1.11.1.13	MnP (RP: 1.0–1.2 V) transfer one electron to Mn2+ to generate Mn3+ which upon chelation by carboxylic acids (e.g. oxalates) becomes a diffusible oxidant that abstracts electrons from aromatic compounds to generate radicals.
Versatile Peroxidase (VP) EC 1.11.1.16,	VP (RP: 1.4–1.5 V) exhibit broad substrate specificity and combine activities of both LiP and MnP such as the high-redox potential of LiP and the Mn2+ binding pocket of MnP.
Dye-decolorizing Peroxidases (DyP) EC 1.11.1.19	DyP (RP: 1.2–1.5 V) are secreted peroxidases that can oxidize a broad range of aromatic compounds and compounds with conjugated double bonds; DyP are particularly known for their oxidation of various recalcitrant anthraquinone dyes; DyP natural substrates and functions are not known but they may play a role in lignin degradation despite having a lower redox potential than LiP. The structural fold of DyPs is distinct from other peroxidases as their heme binding pocket is located in a C-terminal domain. DyPs are evolutionary related to chlorite dismutases; their catalytic mechanism has yet to be fully elucidated.
Heme-thiolate Peroxygenase EC 1.11.2	Incorporation of one oxygen from H2O2 into substrate: [S]H + H2O2 ⇔ [P]-OH + H2O
Unspecific Peroxygenase (UPO) EC 1.11.2.1	UPOs (RP: 0.9–1.2 V) are heme-containing enzymes with a P450 spectrum. They catalyze similar reactions than P450 monooxygenases by using the P450 “peroxide shunt” pathway. UPOs oxidize many aromatic, aliphatic and heterocyclic substrates.
Chloroperoxygenase (CPO) EC 1.11.1.10	CPOs are heme-containing enzymes with P450 characteristics that catalyzes one and two electron oxidations of halides, hydroxylation/epoxidation of benzylic carbons, double bonds of linear and cyclic alkanes, organic sulfides and halogenated substrates CPOs unlike UPOs do not oxidize aromatic ring carbons or alkanes.
Peroxide generating enzymes	Transfer of two electrons to O2: [S] + O2 ⇔ [S]ox+ H2O2 Generate H2O2 for i) non-enzymatic generation of diffusible oxidants via Fenton chemistry and ii) various peroxidases and peroxygenases.
Glucose-methanol-choline (GMC) oxidoreductase EC 1.1.X.X, AA3	GMCs are flavin containing enzymes that catalyze the oxidation of a wide range of substrates in a first half reaction and reduce O2 to H2O2 in a second half reaction to regenerate the oxidized flavin co-factor: [S]OH +FAD + O2 ⇔ [S]O + FAD+ H2O2 GMC are a widely distributed family of extra- and intracellular enzymes that includes the aryl-alcohol -, pyranose – and methanol oxidases which generate H2O2 for lignin depolymeration.
Aryl-Alcohol oxidase(AAO) EC 1.1.3.7	AAO oxidize aromatic alcohols.
Pyranose oxidase (Pox) EC1.1.3.10	Pox xatalyzes the regioselective oxidation of aldopyranoses at the C2-position to form the corresponding keto-aldoses. Located in the periplasmic space of fungal hyphae.
Copper radical oxidase (CRO) EC 1.1.3, AA5	Reaction: [S]O + 2O2 ⇔ [S]OOH + H2O2 CROs fall into several subfamilies that are widely distributed in Basidiomycota. Functions of most subfamilies uncharacterized
Glyoxyl oxidase (GLX) EC 1.1.3.1	GLC oxidize simple aldehydes to hydroxyl-carbonyls to generate small organic acids as Mn3+ chelators. Their active site is similar to those of galactose oxidase
Multi-copper oxidase EC 1.10.3.X, AA1	Catalyze 4 electron reduction of O2 to H2O: 4 [S]OH + O2 ⇔ 4[S]O + 2H2O
Laccase (LAC) EC 1.10.3.2	LAC contain 4 copper ions of three different types; three copper ions form a trinuclear cluster LACs have moderate redox potentials (RP: 0.4–0.8 V) allowing them to abstract electrons from phenolic compounds to generate phenoxy radicals. LACs catalyze the oxidation of non-phenolic compounds in the presence of mediators
Benzoquinone reductase (BQR) EC 1.6.5.6, AA6	FAD-containing intracellular oxidoreductase that reduces benzoquinones to the corresponding alcohols to fuel extracellular quinone redox cycling for H2O2 and radical generation: benzoquinone + NADPH + H+ ⇔ hydroquinone+ NADP++ H2O
P450 monoxygenase	P450s incorporate oxygen from molecular oxygen into a wide range of substrates: [S] + O2 + NADPH2 ⇔ [P]O + NADP + H2O P450s oxidize unreactive carbons and a play major role in the detoxification of xenobiotics and secondary metabolism. P450 families have been greatly expanded in Basidiomyctoa.
Dioxygenases	Dioxygenases transfer two oxygens from molecular oxygen into substrates: [S] + O2 + NADPH2 ⇔ [P]O2 Lipoxygenases (LOX) are a class of non-heme iron containing oxidoreductases that typically catalyze the regio- and stereoselective insertion of molecular oxygen into cis-polyunsaturated fatty acids to produce compounds involved in signaling and defense. LOX in Basidiomycota are responsible for the generation of oxygenated C8 volatiles that generate the typical mushroom odor.