MNLOX_PLESI
ID MNLOX_PLESI Reviewed; 643 AA.
AC M5EES5; B8ZIU7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:34033194};
DE EC=1.13.11.12 {ECO:0000269|Ref.3, ECO:0000305|PubMed:34033194};
DE AltName: Full=LOXPsa1 {ECO:0000303|Ref.3};
DE AltName: Full=Valencene dioxygenase {ECO:0000303|Ref.2};
DE Short=ValOx {ECO:0000303|Ref.2};
GN Name=LOX1 {ECO:0000303|PubMed:34033194};
OS Pleurotus sapidus (Oyster mushroom) (Agaricus sapidus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=98349;
RN [1] {ECO:0000312|EMBL:CCV01581.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND BIOTECHNOLOGY.
RC STRAIN=DSMZ 8266 {ECO:0000312|EMBL:CCV01581.1};
RX PubMed=22264428; DOI=10.1016/j.biortech.2011.12.097;
RA Zelena K., Krings U., Berger R.G.;
RT "Functional expression of a valencene dioxygenase from Pleurotus sapidus in
RT E. coli.";
RL Bioresour. Technol. 108:231-239(2012).
RN [2] {ECO:0000312|EMBL:CAQ87588.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-643, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND BIOTECHNOLOGY.
RX DOI=10.1016/j.molcatb.2009.07.001;
RA Fraatz M.A., Riemer S.J.L., Stuber R., Kaspera R., Nimtz M., Berger R.G.,
RA Zorn H.;
RT "A novel oxygenase from Pleurotus sapidus transforms valencene to
RT nootkatone.";
RL J. Mol. Catal., B Enzym. 61:202-207(2009).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RX DOI=10.1016/j.molcatb.2012.11.004;
RA Plagemann I., Zelena K., Arendt P., Ringel P.D., Krings U., Berger R.G.;
RT "LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus.";
RL J. Mol. Catal., B Enzym. 87:99-104(2013).
RN [4] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND BIOTECHNOLOGY.
RX PubMed=34033194; DOI=10.1002/cbic.202100183;
RA Krahe N.K., Berger R.G., Kahlert L., Ersoy F.;
RT "Co-Oxidative Transformation of Piperine to Piperonal and 3,4-
RT Methylenedioxycinnamaldehyde by a Lipoxygenase from Pleurotus sapidus.";
RL ChemBioChem 22:2857-2861(2021).
CC -!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic
CC acids to 13S-hydroperoxy fatty acids. {ECO:0000269|PubMed:34033194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC Evidence={ECO:0000269|Ref.3, ECO:0000305|PubMed:34033194};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8X151};
CC Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or
CC Val residue, and a fifth residue, usually Asn, ligate the metal, which
CC binds water to form a catalytic base Mn(2+)OH(2) for hydrogen
CC abstraction. {ECO:0000250|UniProtKB:Q8X151};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.3 uM for linoleic acid (at pH 7.0 and 22 degrees Celsius)
CC {ECO:0000269|Ref.3};
CC Note=kcat is 157 sec(-1) for linoleic acid (at pH 7.0 and 22 degrees
CC Celsius). {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:34033194, ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius (PubMed:34033194). Optimum
CC temperature is 35 degrees Celsius (Ref.3).
CC {ECO:0000269|PubMed:34033194, ECO:0000269|Ref.3};
CC -!- BIOTECHNOLOGY: The oxidation of primary substrates may lead to co-
CC oxidation of other molecules (Ref.2, PubMed:34033194). Cleaves piperine
CC to piperonal and 3,4-methylenedioxycinnamaldehyde (PubMed:34033194).
CC Converts (+)-valencene to (+)-nootkatone, alpha-nootkatol and beta-
CC nootkatol (PubMed:22264428, Ref.2, Ref.3). Converts trans-anethole to
CC p-methoxybenzaldehyde (PubMed:34033194). Converts trans-
CC isomethyleugenol to veratraldehyde (PubMed:34033194). Converts alpha-
CC methylstyrene to acetophenone (PubMed:34033194).
CC {ECO:0000269|PubMed:22264428, ECO:0000269|PubMed:34033194,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAQ87588.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ87588.1; Type=Miscellaneous discrepancy; Note=This sequence differs from that shown at positions 419, 539, 548-551, and 873.; Evidence={ECO:0000305};
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DR EMBL; HF913621; CCV01581.1; -; mRNA.
DR EMBL; FM200795; CAQ87588.1; ALT_INIT; mRNA.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043651; P:linoleic acid metabolic process; IC:UniProtKB.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR SUPFAM; SSF48484; SSF48484; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Manganese; Metal-binding; Oxidoreductase.
FT CHAIN 1..643
FT /note="Manganese lipoxygenase"
FT /id="PRO_0000454734"
FT DOMAIN 166..643
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 325
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 510
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 514
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT BINDING 643
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:G4NAP4"
FT CONFLICT 525
FT /note="P -> S (in Ref. 2; CAQ87588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72324 MW; 07C98AC01B8716D8 CRC64;
MVHNISLSSR KALHNVHLPY MVQLPKPTGY NVALKNAAEG YDKARRMVAW LYDIADYESS
IPQTFTLQQK TDKYTWELSD NFPPHLAVVP PDQSVSAPSI FSPVRLAQTL LIMSSLWYDD
HTDLAPGPEQ NTMQKLTQWN QERHKDQGWL IKDMFNAPNI GLRNDWYTDE VFAQQFFTGP
NSTTITLASD VWLTAFTSEA KAQGKDKVIA LFESAPPNSF YVQDFSDFRR RMGAKPDEEL
FNDSDGAMRY GCAAVALFYL TAMGKLHPLA IIPDYKGSMA ASVTIFNKRT NPLDISVNQA
NDWPWRYAKT CVLSSDWALH EMIIHLNNTH LVEEAVIVAA QRKLSPSHIV FRLLEPHWVV
TLSLNALARS VLIPEVIVPI AGFSAPHIFQ FIRESFTNFD WKSLYVPADL ESRGFPVDQL
NSPKFHNYAY ARDINDMWTT LKKFVSSVLQ DAQYYPDDAS VAGDTQIQAW CDEMRSGMGA
GMTNFPESIT TVDDLVNMVT MCIHIAAPQH TAVNYLQQYY QTFVPNKPSA LFSPLPTSIA
QLQKYTESDL MAALPLNAKR QWLLMAQIPY LLSMQVQEDE NIVTYAANAS TDKDPIIASA
GRQLAADLKK LAAVFLVNSA QLDDQNTPYD VLAPEQLANA IVI
