RNMT_PAPSO
ID RNMT_PAPSO Reviewed; 363 AA.
AC A0A1C9U5X5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Reticuline N-methyltransferase {ECO:0000303|PubMed:27634038};
DE Short=RNMT {ECO:0000303|PubMed:27634038};
DE EC=2.1.1.337 {ECO:0000269|PubMed:27634038};
DE AltName: Full=N-methyltransferase 3 {ECO:0000303|PubMed:27634038};
GN Name=RNMT {ECO:0000303|PubMed:27634038};
GN Synonyms=NMT3 {ECO:0000303|PubMed:27634038};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000312|EMBL:AOR51552.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=27634038; DOI=10.1074/jbc.m116.750893;
RA Morris J.S., Facchini P.J.;
RT "Isolation and characterization of reticuline N-methyltransferase involved
RT in biosynthesis of the aporphine alkaloid magnoflorine in Opium poppy.";
RL J. Biol. Chem. 291:23416-23427(2016).
CC -!- FUNCTION: N-methyltransferase accepting primarily 1-benzylisoquinoline
CC and aporphine substrates possessing a tertiary amine. The preferred
CC substrates are (R)- and (S)-reticuline and (S)-corytuberine, but can
CC also use (R,S)-tetrahydropapaverine, papaverine, (+)-bulbocapnine, (+)-
CC glaucine, (+)-isocorydine, (+)-isothebaine, boldine, noscapine,
CC narcotine hemiacetal and hydrastine as substrates. Involved in the
CC biosynthesis of magnoflorine. {ECO:0000269|PubMed:27634038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-reticuline + S-adenosyl-L-methionine = (S)-tembetarine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51520,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57873,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134199; EC=2.1.1.337;
CC Evidence={ECO:0000269|PubMed:27634038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-reticuline + S-adenosyl-L-methionine = (R)-tembetarine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51516,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58144,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134198; EC=2.1.1.337;
CC Evidence={ECO:0000269|PubMed:27634038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-corytuberine + S-adenosyl-L-methionine = magnoflorine + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:51524, ChEBI:CHEBI:6641,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:81200;
CC EC=2.1.1.337; Evidence={ECO:0000269|PubMed:27634038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-tetrahydropapaverine + S-adenosyl-L-methionine = (R)-N-
CC methyltetrahydropapaverine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134210, ChEBI:CHEBI:134211;
CC EC=2.1.1.337; Evidence={ECO:0000269|PubMed:27634038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-glaucine + S-adenosyl-L-methionine = (S)-N-methylglaucine
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51556,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134212, ChEBI:CHEBI:134213; EC=2.1.1.337;
CC Evidence={ECO:0000269|PubMed:27634038};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-bulbocapnine + S-adenosyl-L-methionine = (S)-N-
CC methylbulbocapnine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134215, ChEBI:CHEBI:134217;
CC EC=2.1.1.337; Evidence={ECO:0000269|PubMed:27634038};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for (S)-reticuline {ECO:0000269|PubMed:27634038};
CC KM=85 uM for (R)-reticuline {ECO:0000269|PubMed:27634038};
CC KM=168 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:27634038};
CC Vmax=39.6 pmol/min/ug enzyme with (S)-reticuline as substrate
CC {ECO:0000269|PubMed:27634038};
CC Vmax=74.8 pmol/min/ug enzyme with (R)-reticuline as substrate
CC {ECO:0000269|PubMed:27634038};
CC Vmax=66.5 pmol/min/ug enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:27634038};
CC Note=kcat is 0.028 sec(-1) with (S)-reticuline as substrate. kcat is
CC 0.053 sec(-1) with (R)-reticuline as substrate. kcat is 0.047 sec(-1)
CC with S-adenosyl-L-methionine as substrate.
CC {ECO:0000269|PubMed:27634038};
CC pH dependence:
CC Optimum pH is 8.5 with (R)-reticuline as substrate. Optimum pH is
CC 7.0-9.0 with (S)-reticuline as substrate.
CC {ECO:0000269|PubMed:27634038};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:27634038};
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems. Detected in leaves
CC and flower buds. {ECO:0000269|PubMed:27634038}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; KX369612; AOR51552.1; -; mRNA.
DR AlphaFoldDB; A0A1C9U5X5; -.
DR SMR; A0A1C9U5X5; -.
DR BRENDA; 2.1.1.337; 4515.
DR GO; GO:0102964; F:S-adenosyl-L-methionine:(S)-corytuberine-N-methyltransferase activity; IEA:RHEA.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..363
FT /note="Reticuline N-methyltransferase"
FT /id="PRO_0000439849"
FT BINDING 96..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT BINDING 132..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT BINDING 159..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q79FX6"
SQ SEQUENCE 363 AA; 41960 MW; B6327BAA0BEDD852 CRC64;
MSTTMETTKI SQQDDLWKNM ELGQISDEEV RRLMKIGIEK RIKWGTKPTQ QEQLAQLLDF
NKSLRGMKMA TEIDTLENHK IYETPESFNQ IIGGKESAGL FTDETTTTME EANTKMMDLY
CERAGLKDGH TILDLGCGAG LLVLHLAKKY KKSKITGITN TSSHKEYILK QCKNLNLSNV
EIILADVTKV DIESTFDRVF VIGLIEHMKN FELFLRKISK WMKDDGLLLL EHLCHKSFSD
HWEPLSEDDW YAKNFFPSGT LVIPSATCLL YFQEDVTVID HWILSGNNFA RSNEVILKRI
DGKIEEVKDI FMSFYGIGRE EAVKLINWWR LLCITANELF KYNNGEEWLI SQLLFKKKLM
TCI
