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Benzyl alcohol O-benzoyltransferase (EC 2.3.1.196) (Benzoyl coenzyme A:benzyl alcohol benzoyl transferase)

 BEBT_CLABR              Reviewed;         456 AA.
Q8GT21;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
10-MAY-2017, entry version 40.
RecName: Full=Benzyl alcohol O-benzoyltransferase;
EC=2.3.1.196;
AltName: Full=Benzoyl coenzyme A:benzyl alcohol benzoyl transferase;
Clarkia breweri (Fairy fans) (Eucharidium breweri).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Myrtales; Onagraceae; Onagroideae;
Onagreae; Clarkia.
NCBI_TaxID=36903;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, SUBUNIT, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, INDUCTION BY WOUNDING, AND FUNCTION.
PubMed=12226525; DOI=10.1104/pp.006460;
D'Auria J.C., Chen F., Pichersky E.;
"Characterization of an acyltransferase capable of synthesizing
benzylbenzoate and other volatile esters in flowers and damaged leaves
of Clarkia breweri.";
Plant Physiol. 130:466-476(2002).
-!- FUNCTION: Probably involved in the formation of benzylbenzoate, a
minor constituent of the floral aroma.
{ECO:0000269|PubMed:12226525}.
-!- CATALYTIC ACTIVITY: Benzoyl-CoA + benzyl alcohol = CoA + benzyl
benzoate. {ECO:0000269|PubMed:12226525}.
-!- ENZYME REGULATION: Inhibited by magnesium, calcium, cobalt, zinc
and copper. {ECO:0000269|PubMed:12226525}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=46.8 uM for benzyl alcohol (with benzoyl-CoA as cosubstrate)
{ECO:0000269|PubMed:12226525};
KM=97.8 uM for cinnamyl alcohol (with benzoyl-CoA as
cosubstrate) {ECO:0000269|PubMed:12226525};
KM=20.5 uM for benzoyl-CoA (with benzyl alcohol as cosubstrate)
{ECO:0000269|PubMed:12226525};
KM=464 uM for cinnamoyl-CoA (with benzyl alcohol as cosubstrate)
{ECO:0000269|PubMed:12226525};
KM=818 uM for acetyl-CoA (with benzyl alcohol as cosubstrate)
{ECO:0000269|PubMed:12226525};
pH dependence:
Optimum pH is 7.7. {ECO:0000269|PubMed:12226525};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12226525}.
-!- TISSUE SPECIFICITY: Highly expressed in stigma. Detected in
stamens, sepals, petals and style. Bearly expressed in leaves.
{ECO:0000269|PubMed:12226525}.
-!- DEVELOPMENTAL STAGE: Highly expressed in the stigma of unopened
flowers, peaks on day 1 postanthesis and drops rapidly on day 2
postanthesis when the stigma becomes receptive (at protein level).
{ECO:0000269|PubMed:12226525}.
-!- INDUCTION: Up-regulated by wounding. Expression peaks 6 hours
after wonding, decreasing afterward.
{ECO:0000269|PubMed:12226525}.
-!- SIMILARITY: Belongs to the plant acyltransferase family.
{ECO:0000305}.
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EMBL; AF500200; AAN09796.1; -; mRNA.
ProteinModelPortal; Q8GT21; -.
SMR; Q8GT21; -.
KEGG; ag:AAN09796; -.
KO; K19861; -.
BRENDA; 2.3.1.196; 1437.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
InterPro; IPR003480; Transferase.
Pfam; PF02458; Transferase; 1.
1: Evidence at protein level;
Acyltransferase; Transferase.
CHAIN 1 456 Benzyl alcohol O-benzoyltransferase.
/FTId=PRO_0000409590.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255}.
ACT_SITE 380 380 Proton acceptor. {ECO:0000255}.
SEQUENCE 456 AA; 50650 MW; E335098512DCE27A CRC64;
MAHDQSLSFE VCRRKPELIR PAKQTPHEFK KLSDVEDQEG LRFQIPVIQF YKHNNESMQE
RDPVQVIREG IARALVYYYP FAGRLREVDG RKLVVECTGE GVMFIEADAD VTLEQFGDAL
QPPFPCFDQL LFDVPGSGGI LDSPLLLIQV TRLKCGSFIF ALRLNHTMAD AAGIVLFMKA
VGEMARGAAT PSTLPVWDRH ILNARVPPQV TFNHREYEEV KGTIFTPFDD LAHRSFFFGS
TEISAMRKQI PPHLRSCSTT IEVLTACLWR CRTLAIKPNP DEEVRMICIV NARSKFNPPL
PDGYYGNAFA IPAAVTTAGK LCNNPLGFAL ELIRKAKREV TEEYMHSVAD LMVATGRPHF
TVVNTYLVSD VTRAGFGEVD FGWGEAVYGG PAKGGVGVIP GVTSFYIPLR NRQGEKGIVL
PICLPSAAME IFAEALNNTL NGKEIEIAKH FTQSSL


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