CXE1_ACTER
ID CXE1_ACTER Reviewed; 335 AA.
AC Q0ZPV7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Carboxylesterase 1;
DE Short=AeCXE1;
DE EC=3.1.1.1;
GN Name=CXE1;
OS Actinidia eriantha (Velvet vine) (Actinidia fulvicoma var. lanata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=165200;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Marshall S.D., Oakeshott J.G., Russell R.J., Plummer K.M., Newcomb R.D.;
RT "Biochemical characterization and comparison of plant CXE carboxylesterases
RT from Actinidia spp., Arabidopsis thaliana, and Malus pumila.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF NATIVE ENZYME AND COMPLEX WITH
RP PARAOXON INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=17256879; DOI=10.1021/bi062046w;
RA Ileperuma N.R., Marshall S.D., Squire C.J., Baker H.M., Oakeshott J.G.,
RA Russell R.J., Plummer K.M., Newcomb R.D., Baker E.N.;
RT "High-resolution crystal structure of plant carboxylesterase AeCXE1, from
RT Actinidia eriantha, and its complex with a high-affinity inhibitor
RT paraoxon.";
RL Biochemistry 46:1851-1859(2007).
CC -!- FUNCTION: Carboxylesterase acting on esters with varying acyl chain
CC length. {ECO:0000269|PubMed:17256879}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000269|PubMed:17256879};
CC -!- ACTIVITY REGULATION: Is inhibited by the organophosphates paraoxon and
CC dimethylchlorophosphate (DMCP). {ECO:0000269|PubMed:17256879}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.3 uM for 4-methylumbelliferyl acetate
CC {ECO:0000269|PubMed:17256879};
CC KM=16.7 uM for 4-methylumbelliferyl butyrate
CC {ECO:0000269|PubMed:17256879};
CC KM=19.1 uM for 4-methylumbelliferyl heptanoate
CC {ECO:0000269|PubMed:17256879};
CC KM=6.34 uM for 4-methylumbelliferyl octanoate
CC {ECO:0000269|PubMed:17256879};
CC KM=0.117 uM for 4-methylumbelliferyl laureate
CC {ECO:0000269|PubMed:17256879};
CC KM=0.024 uM for 4-methylumbelliferyl palmitate
CC {ECO:0000269|PubMed:17256879};
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; DQ279914; ABB89013.1; -; mRNA.
DR PDB; 2O7R; X-ray; 1.40 A; A=1-335.
DR PDB; 2O7V; X-ray; 2.30 A; A=1-335.
DR PDBsum; 2O7R; -.
DR PDBsum; 2O7V; -.
DR AlphaFoldDB; Q0ZPV7; -.
DR SMR; Q0ZPV7; -.
DR ESTHER; actde-CXE1; Plant_carboxylesterase.
DR PRIDE; Q0ZPV7; -.
DR BRENDA; 3.1.1.1; 9380.
DR SABIO-RK; Q0ZPV7; -.
DR EvolutionaryTrace; Q0ZPV7; -.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Serine esterase.
FT CHAIN 1..335
FT /note="Carboxylesterase 1"
FT /id="PRO_0000403482"
FT MOTIF 90..92
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 169
FT /evidence="ECO:0000305"
FT ACT_SITE 276
FT /evidence="ECO:0000305"
FT ACT_SITE 306
FT /evidence="ECO:0000305"
FT BINDING 92..93
FT /ligand="paraoxon"
FT /ligand_id="ChEBI:CHEBI:27827"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000305|PubMed:17256879,
FT ECO:0007744|PDB:2O7V"
FT BINDING 169
FT /ligand="paraoxon"
FT /ligand_id="ChEBI:CHEBI:27827"
FT /ligand_note="inhibitor"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:17256879,
FT ECO:0007744|PDB:2O7V"
FT BINDING 170
FT /ligand="paraoxon"
FT /ligand_id="ChEBI:CHEBI:27827"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000305|PubMed:17256879,
FT ECO:0007744|PDB:2O7V"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2O7R"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2O7R"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2O7R"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:2O7R"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2O7R"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:2O7R"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2O7R"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:2O7R"
SQ SEQUENCE 335 AA; 37052 MW; CA859F19267B8434 CRC64;
MSNDHLETTG SSDPNTNLLK YLPIVLNPDR TITRPIQIPS TAASPDPTSS SPVLTKDLAL
NPLHNTFVRL FLPRHALYNS AKLPLVVYFH GGGFILFSAA STIFHDFCCE MAVHAGVVIA
SVDYRLAPEH RLPAAYDDAM EALQWIKDSR DEWLTNFADF SNCFIMGESA GGNIAYHAGL
RAAAVADELL PLKIKGLVLD EPGFGGSKRT GSELRLANDS RLPTFVLDLI WELSLPMGAD
RDHEYCNPTA ESEPLYSFDK IRSLGWRVMV VGCHGDPMID RQMELAERLE KKGVDVVAQF
DVGGYHAVKL EDPEKAKQFF VILKKFVVDS CTTKL
