OMT2_HUMLU
ID OMT2_HUMLU Reviewed; 360 AA.
AC B0ZB56;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Xanthohumol 4-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.339 {ECO:0000269|PubMed:18223037};
DE AltName: Full=Desmethylxanthohumol 6'-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.338 {ECO:0000269|PubMed:18223037};
DE AltName: Full=Isoliquiritigenin 2'-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.154 {ECO:0000269|PubMed:18223037};
DE AltName: Full=O-methyltransferase 2 {ECO:0000303|PubMed:18223037};
DE Short=HlOMT2 {ECO:0000303|PubMed:18223037};
GN Name=OMT2 {ECO:0000303|PubMed:18223037};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBSTRATE
RP SPECIFICITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP AND PATHWAY.
RC TISSUE=Lupulin gland;
RX PubMed=18223037; DOI=10.1105/tpc.107.055178;
RA Nagel J., Culley L.K., Lu Y., Liu E., Matthews P.D., Stevens J.F.,
RA Page J.E.;
RT "EST analysis of hop glandular trichomes identifies an O-methyltransferase
RT that catalyzes the biosynthesis of xanthohumol.";
RL Plant Cell 20:186-200(2008).
RN [2]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of prenylated phenolics natural
CC products which contribute to the bitter taste of beer and display broad
CC biological activities (Probable). O-methyltransferase with a low
CC substrate selectivity (PubMed:18223037). Methylates chalconaringenin,
CC desmethylxanthohumol, xanthohumol, isoliquiritigenin, butein, 2',4-
CC dihydroxychalcone, resveratrol, genistein and guaiacol
CC (PubMed:18223037). Catalyzes the biosynthesis of 2',4'-dihydroxy-4,6'-
CC dimethoxy-3'-prenylchalcone (4-O-methylxanthohumol) (PubMed:18223037).
CC {ECO:0000269|PubMed:18223037, ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + xanthohumol = 4-O-methylxanthohumol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134289, ChEBI:CHEBI:139273; EC=2.1.1.339;
CC Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51705;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + xanthohumol; Xref=Rhea:RHEA:51696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134289, ChEBI:CHEBI:134302; EC=2.1.1.338;
CC Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51697;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isoliquiritigenin + S-adenosyl-L-methionine = 2'-O-
CC methylisoliquiritigenin + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21608, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:77948, ChEBI:CHEBI:519567; EC=2.1.1.154;
CC Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21609;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-resveratrol = 3-methoxy-4',5-
CC dihydroxy-trans-stilbene + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32111, ChEBI:CHEBI:15378, ChEBI:CHEBI:45713,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:63672;
CC Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32112;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- ACTIVITY REGULATION: Inhibited by S-adenosyl homocysteine.
CC {ECO:0000269|PubMed:18223037}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=237 uM for chalconaringenin {ECO:0000269|PubMed:18223037};
CC KM=23 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037};
CC KM=31 uM for xanthohumol {ECO:0000269|PubMed:18223037};
CC KM=19 uM for resveratrol {ECO:0000269|PubMed:18223037};
CC KM=34 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037};
CC Vmax=914 pmol/sec/mg enzyme with chalconaringenin as substrate
CC {ECO:0000269|PubMed:18223037};
CC Vmax=468 pmol/sec/mg enzyme with desmethylxanthohumol as substrate
CC {ECO:0000269|PubMed:18223037};
CC Vmax=451 pmol/sec/mg enzyme with xanthohumol as substrate
CC {ECO:0000269|PubMed:18223037};
CC Vmax=908 pmol/sec/mg enzyme with resveratrol as substrate
CC {ECO:0000269|PubMed:18223037};
CC Vmax=402 pmol/sec/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:18223037};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18223037};
CC Temperature dependence:
CC Optimum temperature is 39 degrees Celsius.
CC {ECO:0000269|PubMed:18223037};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18223037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0ZB55}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lupulin glands. Detected in
CC cones, male flowers and roots. {ECO:0000269|PubMed:18223037}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; EU309726; ABZ89566.1; -; mRNA.
DR AlphaFoldDB; B0ZB56; -.
DR SMR; B0ZB56; -.
DR KEGG; ag:ABZ89566; -.
DR BRENDA; 2.1.1.339; 2716.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033802; F:isoliquiritigenin 2'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..360
FT /note="Xanthohumol 4-O-methyltransferase"
FT /id="PRO_0000439265"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 360 AA; 39792 MW; 4690E1EC6CF49CF3 CRC64;
MELARNDQTE AALRGEANVW KSINGIADFM VMKCALELRI PDIVHSHSAP ITLAQIASSV
PDSPSLNLSY LSRIMRLLVR RKIFSQHKSL DGEEVLYGPT HSSRLLLSKT TLPDQVTLAP
FVAFMTHPYL SAPWSCLARC VKEGGNGFEM VHGGRQLWDL SPGNPEFNKV FNDGMASTAR
ITTMAILSEY RDVFCGICSL VDVGGEFGGS ISAIVKSHPH IKGINYDLPH VVATAPTYTG
LVSHVGGNMF EWIPTAVAVF MKWILHDWAD EDCVKILKNC RRAMPEKGGK IIIVDIVLEP
EGNGLFDDAA VMLDIALMAL TRGKERTEKE WKRVLEEGGF PRYQILKIPA LTSVIEAYPQ
