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Methanol O-anthraniloyltransferase (EC 2.3.1.232) (Anthraniloyl-CoA:methanol acyltransferase) (Benzyl alcohol O-benzoyltransferase) (EC 2.3.1.196)

 ACMAT_VITLA             Reviewed;         449 AA.
Q3ZPN4;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
12-SEP-2018, entry version 30.
RecName: Full=Methanol O-anthraniloyltransferase;
EC=2.3.1.232;
AltName: Full=Anthraniloyl-CoA:methanol acyltransferase;
AltName: Full=Benzyl alcohol O-benzoyltransferase;
EC=2.3.1.196;
Name=AMAT;
Vitis labrusca (Concord grape).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; Vitales; Vitaceae; Vitis.
NCBI_TaxID=103355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
PubMed=16262710; DOI=10.1111/j.1365-313X.2005.02552.x;
Wang J., De Luca V.;
"The biosynthesis and regulation of biosynthesis of Concord grape
fruit esters, including 'foxy' methylanthranilate.";
Plant J. 44:606-619(2005).
-!- FUNCTION: Acyltransferase that catalyzes the formation of methyl
anthranilate, a compound implicated in the 'foxy' odor character
of Concord grapes. Can use a variety of alcohol substrates when
assayed with both benzoyl-CoA and anthraniloyl-CoA.
{ECO:0000269|PubMed:16262710}.
-!- CATALYTIC ACTIVITY: Anthraniloyl-CoA + methanol = CoA + O-methyl
anthranilate. {ECO:0000269|PubMed:16262710}.
-!- CATALYTIC ACTIVITY: Benzoyl-CoA + benzyl alcohol = CoA + benzyl
benzoate. {ECO:0000269|PubMed:16262710}.
-!- ACTIVITY REGULATION: K(+), Ca(2+), Mg(2+) and Mn(2+) increase
enzyme activity while Cu(2+) and Zn(2+) inactivate the enzyme.
{ECO:0000269|PubMed:16262710}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11.8 uM for benzoyl-CoA (with native enzyme, in the presence
of benzyl alcohol) {ECO:0000269|PubMed:16262710};
KM=2.51 uM for anthraniloyl-CoA (with native enzyme, in the
presence of methanol) {ECO:0000269|PubMed:16262710};
KM=14.97 uM for methanol (with native enzyme, in the presence of
anthraniloyl-CoA) {ECO:0000269|PubMed:16262710};
KM=8.42 uM for benzoyl-CoA (with recombinant enzyme, in the
presence of benzyl alcohol) {ECO:0000269|PubMed:16262710};
KM=4.78 uM for anthraniloyl-CoA (with recombinant enzyme, in the
presence of methanol) {ECO:0000269|PubMed:16262710};
KM=31.8 uM for methanol (with recombinant enzyme, in the
presence of anthraniloyl-CoA) {ECO:0000269|PubMed:16262710};
Note=Kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with
native enzyme). Kcat is 0.022 sec(-1) with anthraniloyl-CoA as
substrate (with native enzyme). Kcat is 0.0035 sec(-1) with
methanol as substrate (with native enzyme). Kcat is 0.045 sec(-
1) with benzoyl-CoA as substrate (with recombinant enzyme). Kcat
is 0.01 sec(-1) with anthraniloyl-CoA as substrate (with
recombinant enzyme). Kcat is 0.0058 sec(-1) with methanol as
substrate (with recombinant enzyme).;
pH dependence:
Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16262710};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16262710}.
-!- TISSUE SPECIFICITY: Expressed in berry outer mesocarp, but not in
berry skin. {ECO:0000269|PubMed:16262710}.
-!- DEVELOPMENTAL STAGE: Expression starts when the berries began to
change the color. It increases throughout berry development to
reach a maximum level in very mature berries.
{ECO:0000269|PubMed:16262710}.
-!- MISCELLANEOUS: No AMAT activity can be detected in Vitis vinifera
grapes. {ECO:0000305|PubMed:16262710}.
-!- SIMILARITY: Belongs to the plant acyltransferase family.
{ECO:0000305}.
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EMBL; AY705388; AAW22989.1; -; mRNA.
ProteinModelPortal; Q3ZPN4; -.
SMR; Q3ZPN4; -.
KEGG; ag:AAW22989; -.
KO; K19861; -.
BRENDA; 2.3.1.196; 13227.
BRENDA; 2.3.1.232; 13227.
SABIO-RK; Q3ZPN4; -.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
Gene3D; 3.30.559.10; -; 2.
InterPro; IPR023213; CAT-like_dom_sf.
InterPro; IPR003480; Transferase.
Pfam; PF02458; Transferase; 1.
1: Evidence at protein level;
Acyltransferase; Direct protein sequencing; Transferase.
CHAIN 1 449 Methanol O-anthraniloyltransferase.
/FTId=PRO_0000423915.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255}.
ACT_SITE 383 383 Proton acceptor. {ECO:0000255}.
SEQUENCE 449 AA; 50182 MW; 443AC243353D93F4 CRC64;
MASPSSPLVF SVNRCVPQIV RPANPTPREV KQLSDIDDQE GRRFQIPVIM FYRNNPLMEG
KDPVKVIREA LGKALVYYYP FAGRLIEGDN RKLMVDCTGE GVLFIEADAD TTLENLGDAI
QPMCPCFEEL LYDVPGSTTI LGSPLILIQV TRLRCGGFIF ALRLNHTMSD AAGLIQFLDT
IGEMAQGLSV PSLLPIWQRE LLNARNPPRI TRIHHEYEKV TNTKGTLMAM DENSLVHRSF
FFGREEIRAL RNRLPASLGA CSTFEVLMAC VWRCRTIAFA VDPDEVVRIS CIINMRGKHG
FELPPGYYGN AFVTPASITK AGMLCKNPLE FAIRLVKKAK AEMSQEYIKS VADLMVIKGR
PLFTQPGNFT VSDVTRAGLG EVDFGWGKPV YGGVARACPI ISFRMLFRNS KGEEGSVIPI
WLPPPVMERF EQELKRMTKK AELLITSML


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