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[1]
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NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-43; 133-146; 186-201 AND 297-313, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PYROGLUTAMATE FORMATION AT GLN-31, AND MASS SPECTROMETRY.
STRAIN=cv. Envy;
TISSUE=Callus;
DOI=10.1104/pp.105.069674; PubMed=16258008 [NCBI, ExPASy, EBI, Israel, Japan]
Gabaldon C.,
Lopez-Serrano M.,
Pedreno M.A.,
Barcelo A.R.;
"Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis.";
Plant Physiol. 139:1138-1154(2005).
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- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Involved in the synthesis of highly polymerized lignins.
- CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=241 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme); | | KM=432 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme); | | KM=83 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme); | | KM=124 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme); | | KM=15 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme); | | KM=13 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme); | | Note=The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol; | |
- SUBCELLULAR LOCATION: Secreted (By similarity).
- TISSUE SPECIFICITY: Expressed in tracheary elements, roots, young and old hypocotyls, and stems in the partially glycosylated form and in roots and young hypocotyls in the fully glycosylated form. None of the isoforms is significantly expressed in leaves or cotyledons.
- PTM: N-glycosylated.
- MASS SPECTROMETRY: Mass=31460; Method=MALDI; Range=30-321; Note=Deglycosylated form; Source=PubMed:16258008;.
- MASS SPECTROMETRY: Mass=33440; Method=MALDI; Range=30-321; Note=Partially glycosylated form; Source=PubMed:16258008;.
- MASS SPECTROMETRY: Mass=34700; Method=MALDI; Range=30-321; Note=Fully glycosylated form; Source=PubMed:16258008;.
- SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
- CAUTION: Four genes are encoding the same mature protein that may have different glycosylation degree. The two precursors produced differ by only one amino acid located in the signal peptide.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 321 AA [This is the length of the unprocessed precursor] |
Molecular weight: 34233 Da [This is the MW of the unprocessed precursor] |
CRC64: 620A21D02479F7F3 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSYHKSSGTT LMVPLFMLLI SVNYFMSCNA QLSTTFYDTT CPTALSTIRT SIRSSVSSNR
70 80 90 100 110 120
RNAALVIRLL FHDCFVQGCD ASLLLSGAGS ERASPANDGV LGYEVIDAAK AAVERVCPGV
130 140 150 160 170 180
VSCADILAVA ARDASVAVGG PSWTVRLGRR DSTTSNAAQA ATDLPRGNMV LSQLISNFAN
190 200 210 220 230 240
KGLNTREMVA LSGSHTLGQA RCIRFRGRIY NSTLRIEPNF NRSLSQACPP TGNDATLRPL
250 260 270 280 290 300
DLVTPNSFDN NYYRNLVTSR GLLISDQVLF NADSTDSIVT EYVNNPATFA ADFAAAMVKM
310 320
SEIGVVTGTS GIVRTLCGNP S
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Q4W1I9 in FASTA format |
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