View source for Auxiliary Activity Family 5

{{CuratorApproved}}
* [[Author]]: ^^^Maria Cleveland^^^ and ^^^Yann Mathieu^^^
* [[Responsible Curator]]:  ^^^Harry Brumer^^^
----

<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
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{| {{Prettytable}} 
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|{{Hl2}} colspan="2" align="center" |'''Auxiliary Activity Family AA5'''
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|'''Fold'''    
|Seven-bladed β-propeller 
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|'''Mechanism'''
|Copper Radical Oxidase
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|'''Active site residues'''
|known
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
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| colspan="2" |{{CAZyDBlink}}AA5.html
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== Substrate Specificities ==
Enzymes from Auxiliary Activity Family 5 (AA5) are mononuclear copper-radical oxidases (CROs) that perform the two-electron oxidation of substrates using oxygen as the final electron acceptor ([{{EClink}}1.1.3.- EC 1.1.3.-]) <cite>Kersten2014</cite>. AA5 members are further classified into two major subfamilies <cite>Levasseur2013</cite>. Subfamily AA5_1 contains characterized glyoxal oxidases ([{{EClink}}1.2.3.15 EC 1.2.3.15]) <cite>Daou2017</cite>. Subfamily AA5_2 contains galactose 6-oxidases ([{{EClink}}1.1.3.9 EC 1.1.3.9]), which oxidize the C-6 hydroxyl of diverse galactosides to the corresponding aldehyde   <cite>Whittaker2003,Andberg2017,Cleveland2021b</cite>. AA5_2 also contains the more recently discovered general alcohol oxidases ([{{EClink}}1.1.3.13 EC 1.1.3.13]) <cite>Yin2015,Oide2019,Cleveland2021b</cite> and aryl alcohol oxidases ([{{EClink}}1.1.3.7 EC 1.1.3.7]) <cite>Mathieu2020,Cleveland2021a</cite>. The first biochemically characterized member of AA5 was the galactose 6-oxidase from the phytopathogenic fungus ''Fusarium graminearum'' (previously known as ''Polyporus circinatus'' and ''Cladobotryum (Dactylium) dendroides'' <cite>Ogel1994</cite>), which was originally reported in 1959 following isolation from cultures <cite>Cooper1959 Avigad1962</cite>. Subsequently, the ''Fusarium graminearum'' galactose 6-oxidase became the defining member of AA5_2 <cite>Levasseur2013</cite>.  The first characterized member of what is now known as AA5_1 is the glyoxal oxidase from ''Phanerochaete chrysosporium'', which was likewise isolated from fungal culture <cite>Kersten1987</cite>.

In contrast to their fungal and bacterial counterparts, plant AA5 members do not fall within the two defined subfamilies. An AA5 enzyme from ''Arabidopsis thaliana'' has been demonstrated ''in vivo'' to have galactose 6-oxidase activity and promote cell-to-cell adhesion in the seed coat epidermis <cite>Sola2019</cite>  (see also <cite>Sola2021</cite>). Additionally, a ''Streptomyces lividans'' enzyme, GlxA, which is distantly related to AA5, has been shown to oxidize glycolaldehyde and a deletion mutant showed a loss of glycan accumulation at hyphal tips <cite>Chaplin2015</cite>.

=== AA5_1 ===
The AA5_1 members are generally known as glyoxal oxidases ([{{EClink}}1.2.3.15 EC 1.2.3.15]), characterized examples of which typically accept a range of simple aldehydes, α-hydroxycarbonyl, and α-dicarbonyl compounds as substrates, with the highest activities observed on glyoxal, methylglyoxal and glycolaldehyde <cite>Whittaker1996,Whittaker1999,Kersten1987,Leuthner2004,Kersten2014</cite>. In contrast, two glyoxal oxidases form ''Pycnoporus cinnabarinus'' demonstrated the highest catalytic efficiency on glyoxylic acid <cite>Daou2016</cite>. An apparent distinction between the AA5_1 and AA5_2 subfamilies is that while AA5_1 enzymes catalyze the oxidation of aldehydes to carboxylic acids <cite>Kersten2014</cite>, AA5_2 members oxidize primary alcohols to the corresponding aldehyde (and, in some instances, also oxidize the aldehyde to the acid, albeit much more slowly) <cite>Whittaker2003,Parikka2015</cite>. Consequently, the oxidation of aldehydes by AA5 CROs has been suggested to proceed through the hydrated, ''gem''-diol species <cite>Whittaker1996</cite>.

=== AA5_2 ===
The archetypal CRO and AA5 member is the ''Fusarium graminearum'' galactose 6-oxidase (''Fgr''GalOx), which catalyzes the regioselective oxidation of the C6-hydroxyl group on the monosaccharide galactose ([{{EClink}}1.1.3.7 EC 1.3.3.7]) <cite>Cooper1959 Avigad1962</cite>. The range of substrates oxidized by ''Fgr''GalOx also includes galactosides as methyl beta-galactopyranoside <cite>Paukner2015</cite>, and galactose-containing di-, oligo-, and polysaccharides, including lactose, melibiose, raffinose, galactoxyloglucan, galactomannan and galactoglucomannan <cite>Parikka2015,Parikka2010</cite>. Several other AA5_2 members from ''Fusarium'' species, such as those from ''F. oxysporum'' <cite>Paukner2014</cite>, ''F. sambucinum'' <cite>Paukner2015</cite>, and ''F. acuminatum'' <cite>Alberton2007</cite> have substrate specificities similar to ''Fgr''GalOx.  Other AA5_2 orthologs exhibit specificity for the alpha-galactosyl unit of the di- and trisaccharides mellibiose and raffinose, respectively, over galactose <cite>Andberg2017,Cleveland2021b</cite>.  For many decades following their discovery, galactose 6-oxidase activity was thought to be the defining feature of this family, although a limited ability of ''Fgr''GalOx to oxidize non-carbohydrate alcohols had been noted <cite>Minasian2004 Siebum2006</cite>

In 2015, two AA5_2 orthologs from the fungi ''Colletotrichum graminicola'' and ''Colletotrichum gloeosporioides'' were characterized (''Cgr''AlcOx and ''Cgl''AlcOx, respectively), which were essentially inactive on galactose and galactosides, but efficiently oxidized the hydroxyl group of diverse aliphatic and aromatic primary alcohols <cite>Yin2015</cite>. These enzymes exhibited high catalytic efficiency towards, e.g., ''n''-butan-1-ol, 2,4-hexadiene-1-ol, benzyl alcohol, and cinnamyl alcohol, and were therefore denoted as general alcohol oxidases ([{{EClink}}1.1.3.13 EC 1.3.3.13]) <cite>Yin2015</cite>. Likewise, two AA5_2 members were characterized from the pathogenic fungi ''Pyricularia oryzae'' (''Por''AlcOx) and ''Colletotrichum higginsianum'' (''Chi''AlcOx), which exhibited prominent activity on ''n''-butan-1-ol, ethanol, 1,3-butanediol, and glycerol <cite>Oide2019</cite>. Since then, additional AA5_2 enzymes from various fungi have been characterized as general alcohol oxidases, some of which efficiently oxidize both carbohydrate and non-carbohydrate substrates <cite>Cleveland2021b</cite>.  More specifically, several fungal AA5_2 members, including homologs from ''Colletotrichum/Glomerella'' and ''Fusarium'' species, have been characterized as aryl alcohol oxidases due to predominant specificities toward substituted benzyl alcohols and 5-hydroxymethylfurfural (HMF) (see [{{EClink}}1.1.3.7 EC 1.1.3.7] and [{{EClink}}1.1.3.47 EC 1.1.3.47]) <cite>Mathieu2020 Cleveland2021a Cleveland2021b</cite>.

The specificity of AA5 CROs has been harnessed for a range of biotechnological applications. The earliest examples include glycoprotein labelling via oxidation of galactosyl residues with ''Fgr''GalOx <cite>Roberts1965</cite>. Likewise, ''Fgr''GalOx has been utilized for the production of functionalized carbohydrates from biomass sources <cite>Yalpani1982 Kelleher1986 Schoevaart2004 Leppanen2014 Xu2012 Parikka2012 Mikkonen2014 Derikvand2016</cite>. Several mutants of ''Fgr''GalOx have been developed to attempt to change the substrate preference showing increased activity on glucose (M<sub>3 </sub>with R330K, Q406T, and W290F in M<sub>1</sub> background and Des 3-2 with Q326E, Y329K and R330K in WT background), fructose (R330K in WT background), mannose (variant H<sub>1</sub> with R330K mutation in M<sub>1</sub> background) and N-acetylglucosamine (variant F<sub>2</sub> with R330K, W290F, Q406E, Y405F mutations in M<sub>1</sub> background), secondary alcohols (variant M<sub>3-5 </sub>similar to M<sub>3</sub> with a methionine at the 330 position), and amino alcohols (variants F<sub>2</sub> and M<sub>3-5</sub>) <cite>Sun2002,Lippow2010,Deacon2004,Rannes2011,Escalettes2008,Herter2015, Birmingham2018</cite>. Some of these variants have been explored for the labelling of galactose-containing carbohydrates (M<sub>1</sub>), mannose-containing carbohydrates (H<sub>1</sub>), N-acetylglucosamine and the human xeno-autoantigen N-glycolylneuraminic acid (Neu5Gc) (F<sub>2</sub>) <cite>Rannes2011,Mattey2019</cite>.

The ability of specific AA5 members to oxidize aliphatic and aromatic alcohols to the corresponding aldehydes, including stereoselectively, has biocatalytic applications in chemical production, e.g. for the pharmaceutical and food and fragrance industries <cite>Huffman2019 Toftgaard2015 Birmingham2018 Forget2020 Monosik2012 Schoevaart2004 Ribeaucourt2021a Ribeaucourt2021b Ribeaucourt2021c Roncal2012 Vilim2018</cite>. Similarly, the ability of CROs to convert HMF into the bi-functional precursors diformylfuran (DFF) and 2,5-furandicarboxylic acid (FDCA) may find application in polymer manufacturing <cite>Mathieu2020 Cleveland2021a Cleveland2021b Rosatella2011 Sousa2015 Birmingham2021</cite>.

== Kinetics and Mechanism ==
[[File:CRO_mechanism.png|thumb|400px|right|'''Figure 1.''' Reaction mechanism of copper radical oxidases. A. First half-reaction – oxidation of substrate. B. Second-half reaction – regeneration of active site radical. PT – proton transfer, HAT – hydrogen atom transfer, ET – electron transfer. This figure is reproduced from <cite>Yin2015</cite> (CC BY 4.0).]]
The majority of what is known about the mechanism of AA5 enzymes comes from studies on the archetype, ''Fgr''GalOx.  AA5 enzymes oxidize their substrates through a ping-pong mechanism involving a corresponding reduction of oxygen to hydrogen peroxide mediated by a mononuclear copper center, which is complexed via a distinct, crosslinked tyrosyl-cysteine residue (see below) <cite>Whittaker2003,Whittaker2005,Baron1994,Humphreys2009,Whittaker1993,Whittaker1996,Whittaker1999,Kersten2014</cite>. The first half-reaction results in a two-electron oxidation of the substrate and corresponding reduction of the Cu[II]-tyrosyl radical to a Cu[I]-tyrosine (phenol). The second half-reaction regenerates the oxidation state of the active-site through reduction of molecular oxygen to hydrogen peroxide. Detailed kinetic studies, including kinetic isotope effects, suggest that each half reaction consists of three steps: proton transfer (PT), hydrogen atom transfer (HAT), and electron transfer (ET) <cite>Whittaker2004 Humphreys2009</cite>. Due to its fundamental uniqueness, the mechanism of AA5 CROs has received significant theoretical treatment and the synthesis of many chemical mimetics has been attempted <cite>Wang1998 Itoh2000 Himo2000</cite>.

Practically, AA5 enzymes are conveniently assayed by measuring hydrogen peroxide (co-product) generatation, e.g. in coupled reactions with horseradish peroxidase and a chromogenic substrate.  In preparative reactions, catalase is typically added to prevent accumulation of hydrogen peroxide. AA5 enzymes are prone to inactivation by one-electron reduction to a Cu[I]-tyrosyl radical.  The resulting off-cycle species can be rescued by oxidation by  peroxidases or transition metal ions (ferricyanide, Mg(III), etc.), the inclusion of which in reactions is required to obtain maximal activity and substrate conversion <cite>Kersten1990 Cleveland1975 Hamilton1978 Pedersen2015 Forget2020 Johnson2021 Roncal2012</cite>.

== Catalytic Residues ==
[[File: FgrGalOx_Active_site_CAZY.png|thumb|250px|right|'''Figure 2.''' Active site residues of copper radical oxidases FgrGalOx, Cu ion in orange (PDB ID [{{PDBlink}}1gof 1GOF]). ]]
The redox-active center of AA5 oxidases comprises a copper ion that coordinated by two tyrosine sidechains and two histidine sidechains (in the archetype ''Fgr''GalOx these are Tyr495, Tyr272, His496, and His581, respectively), resulting in a distorted square pyramidal geometry <cite>Ito1991 Ito1994 Yin2015 Mathieu2020</cite>. Based on the copper coordination environment, AA5 proteins are type 2 "non-blue" copper enzymes due to the nitrogen and oxygen ligands <cite>Ito1994</cite>.
The unique feature of AA5 enzymes is the covalently linked equatorial tyrosine with an adjacent cysteine by a thioether bond (Tyr272 and Cys228 in ''Fgr''GalOx) <cite>Ito1991</cite>. The thioether linkage forms spontaneously in the presence of copper and has been shown to stabilize the radical though delocalization onto the equatorial tyrosine during catalysis <cite>Rogers2008</cite>.

Another important feature of AA5 enzymes is a secondary shell amino acid that is located on top of the tyrosine-cysteine cofactor (Trp290 in ''Fgr''GalOx). It has been speculated to be critical in determining the substrate specificity, radical stability and redox activity of ''Fgr''GalOx. W290 has been speculated to be involved in hydrogen bonding to the substrate, the delocalization of the radical located on the Cys-Tyr moiety, and/or protecting the thioether bond from solvent <cite>Whittaker2003,Rogers2007,Kersten2014, Daou2017</cite>. This residue in AA5_1, based on sequence alignments, has been conserved as a histidine <cite>Kersten2014</cite>, while characterized AA5_2 enzymes have an aromatic residue at this position: a tryptophan in galactose oxidases (W290 in ''Fgr''GalOx) <cite>Rogers2007,Cleveland2021b</cite>, a phenylalanine in the ''Colletotrichum'' aliphatic alcohol oxidases <cite>Yin2015</cite>, whereas a tyrosine is present in the raffinose oxidases <cite>Andberg2017,Cleveland2021b</cite> and in the aryl alcohol oxidase from ''Colletotrichum graminicola'' <cite>Mathieu2020</cite>. Furthermore, an AA5 enzyme from ''Streptomyces lividans'' with activity on glycolaldehyde also possesses a tryptophan at this position, similar to ''Fgr''GalOx, however the indole ring has a different orientation compared to ''Fgr''GalOx, which may affect the substrate specificity <cite>Chaplin2015,Chaplin2017</cite>.

In AA5_2 the Tyr-Cys cofactor exhibits an unusually low reduction potential (+275 mV)  <cite>Cowley2016,Thomas2002,Wright2001</cite> compared to unmodified tyrosine in solution (> +800 mV) or in other enzymatic systems <cite>Itoh2000</cite>. Several factors such as the increased stability of the protein free radical through π-stacking with aromatic residues and the electron donating effect of the thioether linkage could contribute to this phenomenon <cite>Jazdzewski2000,Whittaker2003,Rogers2007</cite>. In contrast, AA5_1 have a reduction potential around +640 mV <cite>Whittaker1996</cite> possibly caysed by the substitution of the secondary shell amino acid Trpin AA5_2 with a His in AA5_1 leading to the different oxidizing power of these two subfamilies <cite>Wright2001,Kersten2014</cite>. Furthermore, in the archetypal AA5_2 member, ''Fgr''GalOx, the Trp290His substitution increased the reduction potential of the resulting enzyme from +400 mV to +730 mV <cite>Saysell1997</cite>; however, it also decreased the catalytic efficiency by 1000-fold <cite>Baron1994</cite> and affected the stability of the [Cu2+ Tyr·] metallo-radical complex at neutral pH <cite>Rogers1998</cite>. ''Cgr''AlcOx and ''Cgr''AAO have been speculated to have a lower reduction potential than ''Fgr''GalOx due to their secondary shell amino acid substitutions (Phe in ''Cgr''AlcOx and Tyr in ''Cgr''AAO) <cite>Yin2015,Mathieu2020</cite>.

== Three-dimensional Structures ==
[[File:CRO_tertiary_structure.png|thumb|400px|right|'''Figure 3.''' Crystal structure of copper radical oxidases. A. ''Fgr''GalOx (PDB ID [{{PDBlink}}1gof 1GOF]), Copper ion in orange and B. ''Cgr''AlcOx (PDB ID [{{PDBlink}}5c86 5C86]), Copper ion in grey. This figure is reproduced from <cite>Yin2015</cite> (CC BY 4.0).]]
AA5 members share a core seven-bladed β-propeller fold containing the active site (Figure 3) <cite>Ito1994 Yin2015 Mathieu2020</cite>. The structure of the archetype, ''Fgr''GalOx, was first reported in 1991 and comprises three domains: Domain 1 has a beta-sandwich structure now known as [[Carbohydrate Binding Module Family 32]], Domain 2 is the catalytic domain, and Domain 3 is a small, β-strand domain that packs against the catalytic domain on the side opposite from the active-site <cite>Ito1991 Ito1994</cite>. Notably, the original structural analysis of ''Fgr''GalOx revealed the distinct crosslinked Tyr-Cys active site residue of CROs, provided the first [[CBM32]] tertiary structure, and indicated the ability of Domain 1/[[CBM32]] to bind galactose <cite>Ito1991</cite>.

The [[CBM32]] domain is widely, but not exclusively, conserved among many AA5_2 members, especially from ''Fusarium'' species <cite>Paukner2014 Paukner2015 Faria2019 Cleveland2021b</cite> (including some that do not posses predominant galactose 6-oxidase activity, e.g. ''Fgr''AAO and ''Fox''AAO <cite>Cleveland2021a Cleveland2021b</cite>.) In other cases, PAN  and WSC domains are found in place of the [[CBM32]].  The function of PAN domains in ''Colletotrichum graminicola'' aryl alchohol oxidase and raffinose oxidase is unclear <cite>Mathieu2020 Andberg2017</cite>, while the WSC domain in ''Pyricularia oryzae'' alchohol oxidase was able to bind xylans and fungal chitin/β-1,3-glucan, implicating the involvement of this domain in enzyme anchoring <cite>Oide2019</cite>.  Finally, several general alcohol oxidases (i.e. those with little activity toward galactosides) do not possess a corresponding N-terminal domain, but rather comprise only the core seven-bladed β-propeller and the C-terminal domain (Figure 3) <cite>Yin2015 Oide2019</cite>. Glyoxal oxidases of AA5_1 also appear to lack the N-terminal [[CBM32]] domain found in ''Fgr''GalOx <cite>Whittaker1999</cite>.

== Family Firsts ==
;First AA5_1 enzyme discovered: The glyoxal oxidase from ''Phanerochaete chrysosporium'' discovered in 1987 <cite>Kersten1987</cite>.
;First AA5_2 enzyme discovered:  The archetypal galactose-6 oxidase from ''Fusarium graminearum'' (''Fgr''GalOx) discovered in 1959 <cite>Cooper1959</cite>.
;Copper requirement confirmed: While this first report already established FgrGalOx as a metalloenzyme; its copper requirement was later confirmed <cite>Amaral1963</cite>.
;First 3-D structure: The first crystallography structure of AA5 was of the archetypal ''Fgr''GalOx in 1991 <cite>Ito1991</cite>.

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#Monosik2012 Monosik, R.;  Stredansky, M.;  Tkac, J.; Sturdik, E. (2012) Application of Enzyme Biosensors in Analysis of Food and Beverages. ''Food Anal. Methods.'' '''5''', 40-53. [https://doi.org/10.1007/s12161-011-9222-4 DOI:10.1007/s12161-011-9222-4]
#Huffman2019 pmid=31806816
#Toftgaard2015 Toftgaard Pedersen, A.;  Birmingham, W. R.;  Rehn, G.;  Charnock, S. J.;  Turner, N. J.; Woodley, J. M. (2015) Process Requirements of Galactose Oxidase Catalyzed Oxidation of Alcohols. ''Org. Process Res. Dev.'' '''19''', 1580-1589. [https://doi.org/10.1021/acs.oprd.5b00278 DOI:10.1021/acs.oprd.5b00278]
#McKenna2017 McKenna, S. M.;  Mines, P.;  Law, P.;  Kovacs-Schreiner, K.;  Birmingham, W. R.;  Turner, N. J.;  Leimkühler, S.; Carnell, A. J. (2017) The continuous oxidation of HMF to FDCA and the immobilisation and stabilisation of periplasmic aldehyde oxidase (PaoABC). ''Green Chem.'' '''19''', 4660-4665. [https://doi.org/10.1039/C7GC01696D DOI:10.1039/C7GC01696D]
#Birmingham2021 pmid=34400632

#Ribeaucourt2021c Ribeaucourt, D.; Bissaro, B.; Guallar, V.; Yemloul, M.; Haon, M.; Grisel, S.; Alphand, V.; Brumer, H.; Lambert, F.; Berrin, J-G.; Lafond, M. (2021) Comprehensive Insights into the Production of Long Chain Aliphatic Aldehydes Using a Copper-Radical Alcohol Oxidase as Biocatalyst. ''ACS Sustainable Chem. Eng''. '''9''', 4411-4421 [https://doi.org/10.1021/acssuschemeng.0c07 DOI:10.1021/acssuschemeng.0c07]
#Vilim2018 pmid=30176101
</biblio>

[[Category:Auxiliary Activity Families|AA005]]