TRN1_COCOF
ID TRN1_COCOF Reviewed; 273 AA.
AC A7DY56;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Tropinone reductase {ECO:0000303|PubMed:18221363};
DE EC=1.1.1.206 {ECO:0000269|PubMed:18221363};
DE EC=1.1.1.236 {ECO:0000269|PubMed:18221363};
GN Name=TR {ECO:0000303|PubMed:18221363};
OS Cochlearia officinalis (Common scurvygrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Cochlearieae; Cochlearia.
OX NCBI_TaxID=270110 {ECO:0000312|EMBL:CAO02390.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF
RP TYR-209.
RC TISSUE=Leaf;
RX PubMed=18221363; DOI=10.1111/j.1365-313x.2008.03422.x;
RA Brock A., Brandt W., Drager B.;
RT "The functional divergence of short-chain dehydrogenases involved in
RT tropinone reduction.";
RL Plant J. 54:388-401(2008).
RN [2]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
CC -!- FUNCTION: Oxidoreductase having both tropinone reductase I and II
CC activities. Involved in the tropane alkaloids calystegines and
CC cochlearine biosynthesis. Can use tropinone and nortropinone as
CC substrates and produces both tropine and pseudotropine. Able to oxidize
CC pseudotropine in the reverse reaction. {ECO:0000269|PubMed:18221363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + tropine = H(+) + NADPH + tropinone;
CC Xref=Rhea:RHEA:18357, ChEBI:CHEBI:15378, ChEBI:CHEBI:57554,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349;
CC EC=1.1.1.206; Evidence={ECO:0000269|PubMed:18221363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pseudotropine = H(+) + NADPH + tropinone;
CC Xref=Rhea:RHEA:24244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57493,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349;
CC EC=1.1.1.236; Evidence={ECO:0000269|PubMed:18221363};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3290 uM for tropinone {ECO:0000269|PubMed:18221363};
CC KM=2002 uM for nortropinone {ECO:0000269|PubMed:18221363};
CC KM=42 uM for 8-thiabicyclo[3.2.1]octan-3-one
CC {ECO:0000269|PubMed:18221363};
CC KM=2636 uM for quinuclidinone {ECO:0000269|PubMed:18221363};
CC KM=1342 uM for N-propylpiperidin-4-one {ECO:0000269|PubMed:18221363};
CC KM=7583 uM for N-methylpiperidin-4-one {ECO:0000269|PubMed:18221363};
CC KM=13 uM for 3-methylcyclohexanone {ECO:0000269|PubMed:18221363};
CC KM=15 uM for 4-methylcyclohexanone {ECO:0000269|PubMed:18221363};
CC Vmax=0.79 nmol/sec/mg enzyme with tropinone as substrate
CC {ECO:0000269|PubMed:18221363};
CC Vmax=0.59 nmol/sec/mg enzyme with nortropinone as substrate
CC {ECO:0000269|PubMed:18221363};
CC Vmax=1.50 nmol/sec/mg enzyme with 8-thiabicyclo[3.2.1]octan-3-one as
CC substrate {ECO:0000269|PubMed:18221363};
CC Vmax=2.73 nmol/sec/mg enzyme with quinuclidinone as substrate
CC {ECO:0000269|PubMed:18221363};
CC Vmax=22.24 nmol/sec/mg enzyme with N-propylpiperidin-4-one as
CC substrate {ECO:0000269|PubMed:18221363};
CC Vmax=29.53 nmol/sec/mg enzyme with N-methylpiperidin-4-one as
CC substrate {ECO:0000269|PubMed:18221363};
CC Vmax=21.67 nmol/sec/mg enzyme with 3-methylcyclohexanone as substrate
CC {ECO:0000269|PubMed:18221363};
CC Vmax=47.23 nmol/sec/mg enzyme with 4-methylcyclohexanone as substrate
CC {ECO:0000269|PubMed:18221363};
CC pH dependence:
CC Optimum pH is 8.0. The pH has no influence on the tropine to
CC pseudotropine product ratio. {ECO:0000269|PubMed:18221363};
CC -!- MISCELLANEOUS: The hydroxyphenyl ring arrangement of Tyr-209 determines
CC the tropinone orientation and the formation of either tropine or
CC pseudotropine. {ECO:0000305|PubMed:18221363}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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DR EMBL; AM748271; CAO02390.1; -; mRNA.
DR AlphaFoldDB; A7DY56; -.
DR SMR; A7DY56; -.
DR PRIDE; A7DY56; -.
DR BRENDA; 1.1.1.206; 1550.
DR BRENDA; 1.1.1.236; 1550.
DR SABIO-RK; A7DY56; -.
DR GO; GO:0050356; F:tropine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050358; F:tropinone reductase activity; IEA:UniProtKB-EC.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR045000; TR.
DR PANTHER; PTHR42898; PTHR42898; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..273
FT /note="Tropinone reductase"
FT /id="PRO_0000432371"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 22..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT MUTAGEN 209
FT /note="Y->S: Loss of tropinone or nortropinone reduction,
FT but faster reduction of cyclohexanones."
FT /evidence="ECO:0000269|PubMed:18221363"
SQ SEQUENCE 273 AA; 29478 MW; B46D2FCDC295871A CRC64;
MANLRESSRD KSRWSLEGMT ALVTGGSKGI GEAVVEELAM LGARVHTCAR DETQLQESLR
EWQAKGFQVT TSVCDVSSRD QREKLMETVS SLFQGKLNIL VNNAGTCITK PTIDYTSEDF
SFLMSTNLES SFHLSQLAHP LLKSSGLGSI VLISSVASVV HVNVGSIYGA TKGAMNQLAR
NLACEWASDS IKVNSVCPGF ISTPLASNYF RNEEFKKEVE NIIPTGRVGE ANEVSSLVAY
LCLPAASYVT GQTICVDGGF SVNGFTFKSL PLR
