C7124_PRUMU
ID C7124_PRUMU Reviewed; 526 AA.
AC A0A068Q609;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Phenylacetaldehyde oxime monooxygenase CYP71AN24 {ECO:0000303|PubMed:25015725};
DE EC=1.14.14.44 {ECO:0000269|PubMed:25015725};
DE AltName: Full=Cytochrome P450 71AN24 {ECO:0000303|PubMed:25015725};
DE AltName: Full=Phenylacetonitrile alpha-monooxygenase CYP71AN24 {ECO:0000303|PubMed:25015725};
DE EC=1.14.14.77 {ECO:0000269|PubMed:25015725};
GN Name=CYP71AN24 {ECO:0000303|PubMed:25015725};
OS Prunus mume (Japanese apricot) (Armeniaca mume).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=102107;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Nanko; TISSUE=Seedling;
RX PubMed=25015725; DOI=10.1007/s11103-014-0225-6;
RA Yamaguchi T., Yamamoto K., Asano Y.;
RT "Identification and characterization of CYP79D16 and CYP71AN24 catalyzing
RT the first and second steps in L-phenylalanine-derived cyanogenic glycoside
RT biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc.";
RL Plant Mol. Biol. 86:215-223(2014).
CC -!- FUNCTION: Involved in L-phenylalanine-derived cyanogenic glycoside
CC biosynthesis, including prunasin and amygdalin defensive agents
CC (PubMed:25015725). Catalyzes the conversion of phenylacetaldoxime
CC (PAOx) and phenylacetonitrile (PAN) into mandelonitrile (MAN)
CC (PubMed:25015725). To a lower extent, can convert various aromatic
CC aldoximes and nitriles; mediates the transformation of 4-
CC hydroxyphenylacetaldoxime, 4-hydroxyphenylacetonitrile, indole-3-
CC acetal-doxime and indole-3-acetonitrile into the corresponding
CC hydroxynitriles, but cannot use the aliphatic compounds 2-
CC methylpropanaloxime and 2-methylpropanenitrile as substrates
CC (PubMed:25015725). {ECO:0000269|PubMed:25015725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-phenylacetaldehyde oxime + O2 + reduced [NADPH--
CC hemoprotein reductase] = (R)-mandelonitrile + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52156, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18450,
CC ChEBI:CHEBI:47793, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.44; Evidence={ECO:0000269|PubMed:25015725};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + phenylacetonitrile + reduced [NADPH--hemoprotein
CC reductase] = (R)-mandelonitrile + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:52164, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18450, ChEBI:CHEBI:25979,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.77;
CC Evidence={ECO:0000269|PubMed:25015725};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for phenylacetaldoxime (in the presence of NADPH at pH 7.6
CC and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC KM=18.5 uM for phenylacetonitrile (in the presence of NADPH at pH 7.6
CC and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC KM=7 uM for 4-hydroxyphenylacetaldoxime (in the presence of NADPH at
CC pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC KM=195.5 uM for 4-hydroxyphenylacetonitrile (in the presence of NADPH
CC at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC KM=8.2 uM for indole-3-acetaldoxime (in the presence of NADPH at pH
CC 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC KM=751.1 uM for indole-3-acetonitrile (in the presence of NADPH at pH
CC 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:25015725};
CC Note=kcat is 46.3 min(-1) with phenylacetaldoxime as substrate (in
CC the presence of NADPH at pH 7.6 and 30 degrees Celsius)
CC (PubMed:25015725). kcat is 24.2 min(-1) with phenylacetonitrile as
CC substrate (in the presence of NADPH at pH 7.6 and 30 degrees Celsius)
CC (PubMed:25015725). kcat is 37 min(-1) with 4-
CC hydroxyphenylacetaldoxime as substrate (in the presence of NADPH at
CC pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is 34 min(-1)
CC with 4-hydroxyphenylacetonitrile as substrate (in the presence of
CC NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is
CC 1.7 min(-1) with indole-3-acetaldoxime as substrate (in the presence
CC of NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is
CC 6.1 min(-1) with indole-3-acetonitrile as substrate (in the presence
CC of NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725).
CC {ECO:0000269|PubMed:25015725};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and leaves.
CC {ECO:0000269|PubMed:25015725}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB920492; BAP15888.1; -; mRNA.
DR RefSeq; NP_001313440.1; NM_001326511.1.
DR AlphaFoldDB; A0A068Q609; -.
DR SMR; A0A068Q609; -.
DR GeneID; 103337951; -.
DR BioCyc; MetaCyc:MON-20057; -.
DR BRENDA; 1.14.14.44; 8044.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Phenylacetaldehyde oxime monooxygenase CYP71AN24"
FT /id="PRO_0000449231"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 465
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 526 AA; 59762 MW; 7DA1BE3D3574F361 CRC64;
MALLTLFNQI WQEGQLQSST SSFNIFLVPI LCLSIFILFS LTRSSSPSEK NRKLKLPPSP
PRLPWIGNLH QLGSFPHRSL RALSKKYGDV MFMHFGKVPT LIVSSAEMAK DVMKTQDIVF
CSRPQTTAPS ILFYDGHDIA FAPYGEYWRQ VRRICVLELL SLKRVHQFQY ARVEEVAELV
SKIRKASASA NGAPINLGEL LVSTSNNIIC RCILGQKFED KEDNWFGETT KELMTQVMSF
SFGDFFPSLK WIDRARGYLA YLKSIWLEFD KFFDKLIDEH KAAQKEGKPR KKDIVDILLD
VQNDGSLDFE LTTSNVKAIL QDMFVGGSDT SWTAAIWLMS ELSQNPRVMK KVQEEVRRVA
GKRGYVEESD INEMKYLTCV IKENLRLHPP APLLLPREAM SDVKLGGFDI PAKTQVFVNA
YAVQRDPKVW DKPDEFMPER FEENNVGFVG QDFELIPFGA GRRVCPGLAF GVASAQYVLA
NMLYWFDWKL PSGGSKLAET LDMSEVYGLT VHKKSPLYLV PTPYSP
