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S-norcoclaurine synthase (EC 4.2.1.78)

 NCS_THLFG               Reviewed;         210 AA.
Q67A25;
20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
05-DEC-2018, entry version 43.
RecName: Full=S-norcoclaurine synthase;
EC=4.2.1.78 {ECO:0000269|PubMed:15447655, ECO:0000269|PubMed:17696451, ECO:0000269|PubMed:19004827};
Flags: Precursor;
Thalictrum flavum subsp. glaucum (Yellow meadow rue).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales;
Ranunculaceae; Thalictroideae; Thalictrum.
NCBI_TaxID=150095;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 112-120 AND 157-169,
TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC
ACTIVITY.
PubMed=15447655; DOI=10.1111/j.1365-313X.2004.02210.x;
Samanani N., Liscombe D.K., Facchini P.J.;
"Molecular cloning and characterization of norcoclaurine synthase, an
enzyme catalyzing the first committed step in benzylisoquinoline
alkaloid biosynthesis.";
Plant J. 40:302-313(2004).
[2]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=17696451; DOI=10.1021/bi700752n;
Luk L.Y.P., Bunn S., Liscombe D.K., Facchini P.J., Tanner M.E.;
"Mechanistic studies on norcoclaurine synthase of benzylisoquinoline
alkaloid biosynthesis: an enzymatic Pictet-Spengler reaction.";
Biochemistry 46:10153-10161(2007).
[3]
PROTEIN SEQUENCE OF 30-34, MASS SPECTROMETRY OF 30-210, AND FUNCTION.
PubMed=17900926; DOI=10.1016/j.pep.2007.07.010;
Berkner H., Engelhorn J., Liscombe D.K., Schweimer K., Woehrl B.M.,
Facchini P.J., Roesch P., Matecko I.;
"High-yield expression and purification of isotopically labeled
norcoclaurine synthase, a Bet v 1-homologous enzyme, from Thalictrum
flavum for NMR studies.";
Protein Expr. Purif. 56:197-204(2007).
[4]
FUNCTION, SUBUNIT, AND 3D-STRUCTURE MODELING OF 30-210.
PubMed=18384289; DOI=10.1042/BJ20080306;
Berkner H., Schweimer K., Matecko I., Rosch P.;
"Conformation, catalytic site, and enzymatic mechanism of the PR10
allergen-related enzyme norcoclaurine synthase.";
Biochem. J. 413:281-290(2008).
[5]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND CRYSTALLIZATION.
PubMed=18391427; DOI=10.1107/S1744309108005678;
Pasquo A., Bonamore A., Franceschini S., Macone A., Boffi A.,
Ilari A.;
"Cloning, expression, crystallization and preliminary X-ray data
analysis of norcoclaurine synthase from Thalictrum flavum.";
Acta Crystallogr. F 64:281-283(2008).
[6]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 17-210 APOPROTEIN AND IN
COMPLEX WITH DOPAMINE AND SUBSTRATE ANALOG P-HYDROXYBENZALDEHYDE,
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-108; GLU-110 AND
LYS-122, AND CATALYTIC ACTIVITY.
PubMed=19004827; DOI=10.1074/jbc.M803738200;
Ilari A., Franceschini S., Bonamore A., Arenghi F., Botta B.,
Macone A., Pasquo A., Bellucci L., Boffi A.;
"Structural basis of enzymatic (S)-norcoclaurine biosynthesis.";
J. Biol. Chem. 284:897-904(2009).
-!- FUNCTION: Involved in the biosynthesis of the common precursor of
all benzylisoquinoline alkaloids such as morphine, sanguinarine,
codeine or berberine. Condenses dopamine and 4-
hydroxyphenylacetaldehyde. {ECO:0000269|PubMed:17696451,
ECO:0000269|PubMed:17900926, ECO:0000269|PubMed:18384289}.
-!- CATALYTIC ACTIVITY:
Reaction=(4-hydroxyphenyl)acetaldehyde + dopamine = (S)-
norcoclaurine + H2O; Xref=Rhea:RHEA:16173, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15621, ChEBI:CHEBI:58253, ChEBI:CHEBI:59905;
EC=4.2.1.78; Evidence={ECO:0000269|PubMed:15447655,
ECO:0000269|PubMed:17696451, ECO:0000269|PubMed:19004827};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=330 uM for 4-hydroxyphenylacetaldehyde
{ECO:0000269|PubMed:15447655, ECO:0000269|PubMed:17696451,
ECO:0000269|PubMed:19004827};
KM=380 uM for dopamine {ECO:0000269|PubMed:15447655,
ECO:0000269|PubMed:17696451, ECO:0000269|PubMed:19004827};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:15447655,
ECO:0000269|PubMed:17696451, ECO:0000269|PubMed:19004827};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:15447655, ECO:0000269|PubMed:17696451,
ECO:0000269|PubMed:19004827};
-!- SUBUNIT: Concentration-dependent dimerization, but mainly
monomeric at concentrations around 10 uM.
{ECO:0000269|PubMed:18384289, ECO:0000269|PubMed:19004827}.
-!- TISSUE SPECIFICITY: Expressed most abundantly in the rhizomes and
to a lesser extent in petioles, roots, leaves and flower buds.
{ECO:0000269|PubMed:15447655}.
-!- MASS SPECTROMETRY: Mass=21179.5; Method=Electrospray; Range=30-
210; Evidence={ECO:0000269|PubMed:17900926};
-!- MISCELLANEOUS: May be a member of a small family of three to five
members.
-!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY376412; AAR22502.1; -; mRNA.
PDB; 2VNE; X-ray; 2.72 A; A/B=17-210.
PDB; 2VQ5; X-ray; 2.09 A; A/B=17-210.
PDB; 5N8Q; X-ray; 2.00 A; A/B/C=34-196.
PDB; 5NON; X-ray; 1.85 A; A/B/C=34-196.
PDBsum; 2VNE; -.
PDBsum; 2VQ5; -.
PDBsum; 5N8Q; -.
PDBsum; 5NON; -.
ProteinModelPortal; Q67A25; -.
SMR; Q67A25; -.
KEGG; ag:AAR22502; -.
KO; K13382; -.
BRENDA; 4.2.1.78; 6259.
EvolutionaryTrace; Q67A25; -.
GO; GO:0050474; F:(S)-norcoclaurine synthase activity; IEA:UniProtKB-EC.
GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:InterPro.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR000916; Bet_v_I/MLP.
InterPro; IPR023393; START-like_dom_sf.
Pfam; PF00407; Bet_v_1; 1.
1: Evidence at protein level;
3D-structure; Alkaloid metabolism; Direct protein sequencing; Lyase;
Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 210 S-norcoclaurine synthase.
/FTId=PRO_0000358941.
REGION 108 110 Dopamine binding. {ECO:0000244|PDB:2VQ5,
ECO:0000269|PubMed:19004827}.
ACT_SITE 122 122 Proton donor. {ECO:0000244|PDB:2VQ5,
ECO:0000269|PubMed:19004827}.
BINDING 141 141 4-hydroxyphenylacetaldehyde.
{ECO:0000244|PDB:2VQ5,
ECO:0000269|PubMed:19004827}.
MUTAGEN 108 108 Y->F: Partial loss of activity.
{ECO:0000269|PubMed:19004827}.
MUTAGEN 110 110 E->A: Partial loss of activity.
{ECO:0000269|PubMed:19004827}.
MUTAGEN 122 122 K->A: Loss of activity.
{ECO:0000269|PubMed:19004827}.
STRAND 21 24 {ECO:0000244|PDB:2VQ5}.
HELIX 37 39 {ECO:0000244|PDB:2VQ5}.
STRAND 42 54 {ECO:0000244|PDB:5NON}.
HELIX 56 63 {ECO:0000244|PDB:5NON}.
TURN 66 71 {ECO:0000244|PDB:5NON}.
HELIX 72 75 {ECO:0000244|PDB:5NON}.
STRAND 80 90 {ECO:0000244|PDB:5NON}.
STRAND 94 99 {ECO:0000244|PDB:5NON}.
STRAND 107 116 {ECO:0000244|PDB:5NON}.
TURN 117 120 {ECO:0000244|PDB:5NON}.
STRAND 121 129 {ECO:0000244|PDB:5NON}.
HELIX 130 133 {ECO:0000244|PDB:5NON}.
STRAND 136 149 {ECO:0000244|PDB:5NON}.
STRAND 152 163 {ECO:0000244|PDB:5NON}.
HELIX 165 167 {ECO:0000244|PDB:5NON}.
HELIX 168 171 {ECO:0000244|PDB:5NON}.
TURN 172 174 {ECO:0000244|PDB:5NON}.
HELIX 178 192 {ECO:0000244|PDB:5NON}.
SEQUENCE 210 AA; 23341 MW; 87A47AA31FC96325 CRC64;
MMKMEVVFVF LMLLGTINCQ KLILTGRPFL HHQGIINQVS TVTKVIHHEL EVAASADDIW
TVYSWPGLAK HLPDLLPGAF EKLEIIGDGG VGTILDMTFV PGEFPHEYKE KFILVDNEHR
LKKVQMIEGG YLDLGVTYYM DTIHVVPTGK DSCVIKSSTE YHVKPEFVKI VEPLITTGPL
AAMADAISKL VLEHKSKSNS DEIEAAIITV


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