[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3112136 [NCBI, ExPASy, EBI, Israel, Japan]
Shibata D.,
Steczko J.,
Dixon J.E.,
Hermodson M.,
Yazdanparast R.,
Axelrod B.;
"Primary structure of soybean lipoxygenase-1.";
J. Biol. Chem. 262:10080-10085(1987).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Bonminori;
TISSUE=Cotyledon;
Fukazawa C.,
Masayoshi M.,
Chikafusa F.;
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] OF 426-752.
DOI=10.1007/BF00020127; AGRICOLA=IND87003970
Start W.G.,
Ma Y.,
Polacco J.C.,
Hildebrand D.F.,
Freyer G.A.,
Altschuler M.;
"Two soybean seed lipoxygenase nulls accumulate reduced levels of lipoxygenase transcripts.";
Plant Mol. Biol. 7:11-23(1986).
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[4]
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SEQUENCE REVISION TO 479-482, AND MUTAGENESIS OF SOME HISTIDINE RESIDUES.
DOI=10.1021/bi00131a022; PubMed=1567851 [NCBI, ExPASy, EBI, Israel, Japan]
Steczko J.,
Donoho G.P.,
Clemens J.C.,
Dixon J.E.,
Axelrod B.;
"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.";
Biochemistry 31:4053-4057(1992).
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[5]
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MUTAGENESIS OF SOME HISTIDINE RESIDUES.
DOI=10.1016/0006-291X(92)90801-Q; PubMed=1497657 [NCBI, ExPASy, EBI, Israel, Japan]
Steczko J.,
Axelrod B.;
"Identification of the iron-binding histidine residues in soybean lipoxygenase L-1.";
Biochem. Biophys. Res. Commun. 186:686-689(1992).
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[6]
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ACTIVE SITE, AND IRON LIGANDS.
DOI=10.1021/bi00076a003; PubMed=8518276 [NCBI, ExPASy, EBI, Israel, Japan]
Minor W.,
Steczko J.,
Bolin J.T.,
Otwinowski Z.,
Axelrod B.;
"Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1.";
Biochemistry 32:6320-6323(1993).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS.
PubMed=8502991 [NCBI, ExPASy, EBI, Israel, Japan]
Boyington J.C.,
Gaffney B.J.,
Amzel L.M.;
"The three-dimensional structure of an arachidonic acid 15-lipoxygenase.";
Science 260:1482-1486(1993).
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[8]
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X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
DOI=10.1021/bi960576u; PubMed=8718858 [NCBI, ExPASy, EBI, Israel, Japan]
Minor W.,
Steczko J.,
Stec B.,
Otwinowski Z.,
Bolin J.T.,
Walter R.,
Axelrod B.;
"Crystal structure of soybean lipoxygenase L-1 at 1.4-A resolution.";
Biochemistry 35:10687-10701(1996).
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[9]
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X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-495 AND GLN-697 IN COMPLEX WITH IRON IONS, AND MUTAGENESIS OF GLN-495 AND GLN-697.
PubMed=11412104 [NCBI, ExPASy, EBI, Israel, Japan]
Tomchick D.R.,
Phan P.,
Cymborowski M.,
Minor W.,
Holman T.R.;
"Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1.";
Biochemistry 40:7509-7517(2001).
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- FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13).
- CATALYTIC ACTIVITY: Linoleate + O2 = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate.
- COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By similarity).
- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
- SUBUNIT: Monomer.
- SUBCELLULAR LOCATION: Cytoplasm.
- INDUCTION: The hydroperoxide product serves to activate the resting enzyme. The activation is accompanied by the oxidation of Fe(2+)entadiene structure. L-1 prefers anionic substrate.
- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-1, L-2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in the hypocotyl/radicle region of the seedling stem.
- SIMILARITY: Belongs to the lipoxygenase family.
- SIMILARITY: Contains 1 lipoxygenase domain.
- SIMILARITY: Contains 1 PLAT domain.
- SEQUENCE CAUTION:
- Sequence=CAA47717.1; Type=Frameshift; Positions=663, 697;
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