EzCatDB: M00041

DB codeM00041
CATH domainDomain 12.60.60.20
Domain 24.10.375.10
Domain 34.10.372.10
Domain 43.10.450.60
Domain 51.20.245.10Catalytic domain
E.C.1.13.11.12
CSA1lnh

CATH domainRelated DB codes (homologues)
2.60.60.20T00253

Enzyme Name
Swiss-protKEGG

P08170P09186
Protein nameSeed lipoxygenase-1Seed lipoxygenase-3lipoxygenase
lipoxidase
carotene oxidase
lipoperoxidase
fat oxidase
lipoxydase
lionoleate:O2 oxidoreductase
SynonymsL-1
EC 1.13.11.12
L-3
EC 1.13.11.12

KEGG pathways
MAP codePathways
MAP00591Linoleic acid metabolism
MAP00592alpha-Linolenic acid metabolism

Swiss-prot:Accession NumberP08170P09186
Entry nameLOX1_SOYBNLOX3_SOYBN
ActivityLinoleate + O(2) = (9Z,11E)-(13S)-13- hydroperoxyoctadeca-9,11-dienoate.Linoleate + O(2) = (9Z,11E)-(13S)-13- hydroperoxyoctadeca-9,11-dienoate.
SubunitMonomer.Monomer.
Subcellular locationCytoplasm.Cytoplasm.
CofactorBinds 1 iron ion per subunit. Iron is tightly bound (By similarity).Binds 1 iron ion per subunit. Iron is tightly bound (By similarity).


CofactorsSubstratesProducts
KEGG-idC00023C01595C00007C04717
CompoundIronLinoleateO2(9Z,11E)-(13S)-13-Hydroperoxyoctadeca-9,11-dienoate
Typeheavy metalfatty acidotherscarbohydrate,fatty acid,lipid
1f8nA01UnboundUnboundUnboundUnbound
1fgmA01UnboundUnboundUnboundUnbound
1fgoA01UnboundUnboundUnboundUnbound
1fgqA01UnboundUnboundUnboundUnbound
1fgrA01UnboundUnboundUnboundUnbound
1fgtA01UnboundUnboundUnboundUnbound
1hu9A01UnboundUnboundUnboundUnbound
1ik3A01UnboundUnboundUnboundUnbound
1jnqA01UnboundUnboundUnboundUnbound
1lnhA01UnboundUnboundUnboundUnbound
1n8qA01UnboundUnboundUnboundUnbound
1no3A01UnboundUnboundUnboundUnbound
1ygeA01UnboundUnboundUnboundUnbound
2sblB01UnboundUnboundUnboundUnbound
1f8nA02UnboundUnboundUnboundUnbound
1fgmA02UnboundUnboundUnboundUnbound
1fgoA02UnboundUnboundUnboundUnbound
1fgqA02UnboundUnboundUnboundUnbound
1fgrA02UnboundUnboundUnboundUnbound
1fgtA02UnboundUnboundUnboundUnbound
1hu9A02UnboundUnboundUnboundUnbound
1ik3A02UnboundUnboundUnboundUnbound
1jnqA02UnboundUnboundUnboundUnbound
1lnhA02UnboundUnboundUnboundUnbound
1n8qA02UnboundUnboundUnboundUnbound
1no3A02UnboundUnboundUnboundUnbound
1ygeA02UnboundUnboundUnboundUnbound
2sblB02UnboundUnboundUnboundUnbound
1f8nA03UnboundUnboundUnboundUnbound
1fgmA03UnboundUnboundUnboundUnbound
1fgoA03UnboundUnboundUnboundUnbound
1fgqA03UnboundUnboundUnboundUnbound
1fgrA03UnboundUnboundUnboundUnbound
1fgtA03UnboundUnboundUnboundUnbound
1hu9A03UnboundUnboundUnboundUnbound
1ik3A03UnboundUnboundUnboundUnbound
1jnqA03UnboundUnboundUnboundUnbound
1lnhA03UnboundUnboundUnboundUnbound
1n8qA03UnboundUnboundUnboundUnbound
1no3A03UnboundUnboundUnboundUnbound
1ygeA03UnboundUnboundUnboundUnbound
2sblB03UnboundUnboundUnboundUnbound
1f8nA04UnboundUnboundUnboundUnbound
1fgmA04UnboundUnboundUnboundUnbound
1fgoA04UnboundUnboundUnboundUnbound
1fgqA04UnboundUnboundUnboundUnbound
1fgrA04UnboundUnboundUnboundUnbound
1fgtA04UnboundUnboundUnboundUnbound
1hu9A04UnboundUnboundUnboundUnbound
1ik3A04UnboundUnboundUnboundUnbound
1jnqA04UnboundUnboundUnboundUnbound
1lnhA04UnboundUnboundUnboundUnbound
1n8qA04UnboundUnboundUnboundUnbound
1no3A04UnboundUnboundUnboundUnbound
1ygeA04UnboundUnboundUnboundUnbound
2sblB04UnboundUnboundUnboundUnbound
1f8nA05Bound:FE2UnboundUnboundUnbound
1fgmA05Bound:_FEUnboundUnboundUnbound
1fgoA05Bound:_FEUnboundUnboundUnbound
1fgqA05Bound:_FEUnboundUnboundUnbound
1fgrA05Bound:_FEUnboundUnboundUnbound
1fgtA05Bound:_FEUnboundUnboundUnbound
1hu9A05Bound:_FEUnboundUnboundAnalogue:4HM
1ik3A05Bound:_FEUnboundUnboundBound:13S
1jnqA05Bound:FE2UnboundUnboundAnalogue:EGT
1lnhA05Bound:FE2UnboundUnboundUnbound
1n8qA05Bound:FE2UnboundUnboundAnalogue:DHB
1no3A05Bound:_FEUnboundUnboundAnalogue:4NC
1ygeA05Bound:_FEUnboundUnboundUnbound
2sblB05Bound:_FEUnboundUnboundUnbound

Active-site residues
resource
literature [13], [48], [54]
pdbCatalytic residuesCofactor-binding residuescomment
1f8nA01       


1fgmA01       


1fgoA01       


1fgqA01       


1fgrA01       


1fgtA01       


1hu9A01       


1ik3A01       


1jnqA01       


1lnhA01       


1n8qA01       


1no3A01       


1ygeA01       


2sblB01       


1f8nA02       


1fgmA02       


1fgoA02       


1fgqA02       


1fgrA02       


1fgtA02       


1hu9A02       


1ik3A02       


1jnqA02       


1lnhA02       


1n8qA02       


1no3A02       


1ygeA02       


2sblB02       


1f8nA03       


1fgmA03       


1fgoA03       


1fgqA03       


1fgrA03       


1fgtA03       


1hu9A03       


1ik3A03       


1jnqA03       


1lnhA03       


1n8qA03       


1no3A03       


1ygeA03       


2sblB03       


1f8nA04       


1fgmA04       


1fgoA04       


1fgqA04       


1fgrA04       


1fgtA04       


1hu9A04       


1ik3A04       


1jnqA04       


1lnhA04       


1n8qA04       


1no3A04       


1ygeA04       


2sblB04       


1f8nA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)

1fgmA05       
HIS 499;HIS 504;HIS 690;       ;ILE 839(Iron binding)
mutant N694H
1fgoA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)
mutant Q495A
1fgqA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)
mutant Q495E
1fgrA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)
mutant Q697E
1fgtA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)
mutant Q697N
1hu9A05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1ik3A05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1jnqA05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1lnhA05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1n8qA05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1no3A05ASN 713
HIS 518;HIS 523;HIS 709;ASN 713;ILE 857(Iron binding)

1ygeA05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)

2sblB05ASN 694
HIS 499;HIS 504;HIS 690;ASN 694;ILE 839(Iron binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.4, p.619-621
[9]Fig.1, p.748
[11]p.1486
[13]p.15021-15022
[14]Fig.1, p.15033
[15]p.3978-3979
[20]p.452-455
[21]p.12890-12891
[22]p.10699-10700
[24]p.137-138
[27]Scheme 1, p.635-636
[28]Fig.3, Fig.11, p.806
[30]Scheme 1, p.41-42
[35]Scheme 1, Scheme 2, p.12225-12226
[42]p.7515-7516
[45]Scheme 1, p.10818-10819
[47]Scheme 1
[52]Fig.1, p.5774
[53]Fig.11, p.2008-2013

references
[1]
PubMed ID6784730
JournalBiochem Biophys Res Commun
Year1981
Volume98
Pages922-9
AuthorsFunk MO, Kim SH, Alteneder AW
TitleFactors affecting the initial rate of lipoxygenase catalysis.
[2]
PubMed ID3026385
JournalBiochem Biophys Res Commun
Year1986
Volume141
Pages614-21
AuthorsConnor HD, Fischer V, Mason RP
TitleA search for oxygen-centered free radicals in the lipoxygenase/linoleic acid system.
[3]
PubMed ID3126736
JournalBiochem Biophys Res Commun
Year1988
Volume151
Pages339-46
AuthorsMansuy D, Cucurou C, Biatry B, Battioni JP
TitleSoybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: different reducing substrates and dehydrogenation of phenidone and BW 755C.
[4]
PubMed ID2537058
JournalArch Biochem Biophys
Year1989
Volume269
Pages208-18
AuthorsDraheim JE, Carroll RT, McNemar TB, Dunham WR, Sands RH, Funk MO Jr
TitleLipoxygenase isoenzymes: a spectroscopic and structural characterization of soybean seed enzymes.
[5]
PubMed ID2115880
JournalJ Biol Chem
Year1990
Volume265
Pages12771-3
AuthorsBoyington JC, Gaffney BJ, Amzel LM
TitleCrystallization and preliminary x-ray analysis of soybean lipoxygenase-1, a non-heme iron-containing dioxygenase.
[6]
PubMed ID2113534
JournalJ Biol Chem
Year1990
Volume265
Pages11352-4
AuthorsSteczko J, Muchmore CR, Smith JL, Axelrod B
TitleCrystallization and preliminary X-ray investigation of lipoxygenase 1 from soybeans.
[7]
PubMed ID2313694
JournalJ Mol Biol
Year1990
Volume211
Pages685-7
AuthorsStallings WC, Kroa BA, Carroll RT, Metzger AL, Funk MO
TitleCrystallization and preliminary X-ray characterization of a soybean seed lipoxygenase.
[8]
PubMed ID1324720
JournalBiochemistry
Year1992
Volume31
Pages7700-6
AuthorsRamachandran S, Carroll RT, Dunham WR, Funk MO Jr
TitleLimited proteolysis and active-site labeling studies of soybean lipoxygenase.
[9]
PubMed ID8224502
JournalBiochem Soc Trans
Year1993
Volume21
Pages744-8
AuthorsBoyington JC, Gaffney BJ, Amzel LM
TitleStructure of soybean lipoxygenase-I.
[10]
CommentsACTIVE SITE, AND IRON LIGANDS
Medline ID93298753
PubMed ID8518276
JournalBiochemistry
Year1993
Volume32
Pages6320-3
AuthorsMinor W, Steczko J, Bolin JT, Otwinowski Z, Axelrod B
TitleCrystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1.
Related Swiss-protP08170
[11]
PubMed ID8347579
JournalBiochemistry
Year1993
Volume32
Pages7686-91
AuthorsSchilstra MJ, Veldink GA, Vliegenthart JF
TitleKinetic analysis of the induction period in lipoxygenase catalysis.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID93276267
PubMed ID8502991
JournalScience
Year1993
Volume260
Pages1482-6
AuthorsBoyington JC, Gaffney BJ, Amzel LM
TitleThe three-dimensional structure of an arachidonic acid 15-lipoxygenase.
Related PDB2sbl
Related Swiss-protP08170
[13]
PubMed ID7999759
JournalBiochemistry
Year1994
Volume33
Pages15017-22
AuthorsKramer JA, Johnson KR, Dunham WR, Sands RH, Funk MO Jr
TitlePosition 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3.
[14]
PubMed ID7999760
JournalBiochemistry
Year1994
Volume33
Pages15023-35
AuthorsScarrow RC, Trimitsis MG, Buck CP, Grove GN, Cowling RA, Nelson MJ
TitleX-ray spectroscopy of the iron site in soybean lipoxygenase-1: changes in coordination upon oxidation or addition of methanol.
[15]
PubMed ID8142401
JournalBiochemistry
Year1994
Volume33
Pages3974-9
AuthorsSchilstra MJ, Veldink GA, Vliegenthart JF
TitleThe dioxygenation rate in lipoxygenase catalysis is determined by the amount of iron (III) lipoxygenase in solution.
[16]
PubMed ID7578097
JournalBiochemistry
Year1995
Volume34
Pages14868-73
AuthorsRamachandran S, Richards-Sucheck TJ, Skrzypczak-Jankun E, Wheelock MJ, Funk MO Jr
TitleCatalysis sensitive conformational changes in soybean lipoxygenase revealed by limited proteolysis and monoclonal antibody experiments.
[17]
PubMed ID7628469
JournalEur J Biochem
Year1995
Volume231
Pages186-91
Authorsvan der Heijdt LM, Schilstra MJ, Feiters MC, Nolting HF, Hermes C, Veldink GA, Vliegenthart JF
TitleChanges in the iron coordination sphere of Fe(II) lipoxygenase-1 from soybeans upon binding of linoleate or oleate.
[18]
PubMed ID7549886
JournalProtein Sci
Year1995
Volume4
Pages1233-5
AuthorsSteczko J, Minor W, Stojanoff V, Axelrod B
TitleCrystallization and preliminary X-ray investigation of lipoxygenase-3 from soybeans.
[19]
PubMed ID7878664
JournalToxicol Appl Pharmacol
Year1995
Volume131
Pages1-12
AuthorsYu WK, Wells PG
TitleEvidence for lipoxygenase-catalyzed bioactivation of phenytoin to a teratogenic reactive intermediate: in vitro studies using linoleic acid-dependent soybean lipoxygenase, and in vivo studies using pregnant CD-1 mice.
[20]
PubMed ID8800477
JournalAnnu Rev Biophys Biomol Struct
Year1996
Volume25
Pages431-59
AuthorsGaffney BJ
TitleLipoxygenases: structural principles and spectroscopy.
[21]
PubMed ID8841132
JournalBiochemistry
Year1996
Volume35
Pages12882-92
AuthorsGlickman MH, Klinman JP
TitleLipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover.
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS)
Medline ID96346062
PubMed ID8718858
JournalBiochemistry
Year1996
Volume35
Pages10687-701
AuthorsMinor W, Steczko J, Stec B, Otwinowski Z, Bolin JT, Walter R, Axelrod B
TitleCrystal structure of soybean lipoxygenase L-1 at 1.4 A resolution.
Related PDB1yge
Related Swiss-protP08170
[23]
PubMed ID8778775
JournalProteins
Year1996
Volume24
Pages275-91
AuthorsPrigge ST, Boyington JC, Gaffney BJ, Amzel LM
TitleStructure conservation in lipoxygenases: structural analysis of soybean lipoxygenase-1 and modeling of human lipoxygenases.
[24]
PubMed ID9547548
JournalAdv Exp Med Biol
Year1997
Volume400A
Pages133-8
AuthorsBoyington JC, Gaffney BJ, Amzel LM
TitleThe three-dimensional structure of soybean lipoxygenase-1: an arachidonic acid 15-lipoxygenase.
[25]
PubMed ID9561173
JournalAdv Exp Med Biol
Year1997
Volume433
Pages371-4
AuthorsSuzuki H, Yamamoto S
TitleMolecular and catalytic properties of mammalian lipoxygenases compared with soybean lipoxygenase-1.
[26]
PubMed ID9295158
JournalBiochim Biophys Acta
Year1997
Volume1347
Pages140-50
AuthorsLopez-Nicolas JM, Bru R, Garcia-Carmona F
TitleKinetic characteristics of the enzymatic conversion in presence of cyclodextrins: study of the oxidation of polyunsaturated fatty acids by lipoxygenase.
[27]
PubMed ID9479444
JournalBiochimie
Year1997
Volume79
Pages629-36
AuthorsPrigge ST, Boyington JC, Faig M, Doctor KS, Gaffney BJ, Amzel LM
TitleStructure and mechanism of lipoxygenases.
[28]
PubMed ID9384534
JournalChem Biol
Year1997
Volume4
Pages795-808
AuthorsSolomon EI, Zhou J, Neese F, Pavel EG
TitleNew insights from spectroscopy into the structure/function relationships of lipoxygenases.
[29]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID97440646
PubMed ID9294864
JournalProteins
Year1997
Volume29
Pages15-31
AuthorsSkrzypczak-Jankun E, Amzel LM, Kroa BA, Funk MO Jr
TitleStructure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme.
Related PDB1lnh
Related Swiss-protP09186
[30]
PubMed ID9639559
JournalBiochem J
Year1998
Volume333
Pages33-43
AuthorsHughes RK, Wu Z, Robinson DS, Hardy D, West SI, Fairhurst SA, Casey R
TitleCharacterization of authentic recombinant pea-seed lipoxygenases with distinct properties and reaction mechanisms.
[31]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
PubMed ID9922163
JournalBiochemistry
Year1998
Volume37
Pages17952-7
AuthorsPham C, Jankun J, Skrzypczak-Jankun E, Flowers RA 2nd, Funk MO Jr
TitleStructural and thermochemical characterization of lipoxygenase-catechol complexes.
Related Swiss-protP09186
[32]
PubMed ID9858760
JournalBiochim Biophys Acta
Year1998
Volume1388
Pages325-36
AuthorsWu Y, Wang ZX
TitleComparison of conformational changes and inactivation of soybean lipoxygenase-1 during urea denaturation.
[33]
PubMed ID10558895
JournalBiochem Biophys Res Commun
Year1999
Volume265
Pages489-93
AuthorsGarcia-Barrado JA, Gata JL, Santano E, Solis JI, Pinto MC, Macias P
TitleThe use of fluorescein 5'-isothiocyanate for studies of structural and molecular mechanisms of soybean lipoxygenase.
[34]
PubMed ID10529238
JournalBiochemistry
Year1999
Volume38
Pages13920-7
AuthorsBegan G, Sudharshan E, Appu Rao AG
TitleChange in the positional specificity of lipoxygenase 1 due to insertion of fatty acids into phosphatidylcholine deoxycholate mixed micelles.
[35]
Medline ID99119225
PubMed ID10493789
JournalBiochemistry
Year1999
Volume38
Pages12218-28
AuthorsRickert KW, Klinman JP
TitleNature of hydrogen transfer in soybean lipoxygenase 1: separation of primary and secondary isotope effects.
[36]
PubMed ID10585402
JournalJ Biol Chem
Year1999
Volume274
Pages35351-8
AuthorsSudharshan E, Rao AG
TitleInvolvement of cysteine residues and domain interactions in the reversible unfolding of lipoxygenase-1.
[37]
PubMed ID10769137
JournalBiochemistry
Year2000
Volume39
Pages4801-7
AuthorsMogul R, Johansen E, Holman TR
TitleOleyl sulfate reveals allosteric inhibition of soybean lipoxygenase-1 and human 15-lipoxygenase.
[38]
PubMed ID10672019
JournalEur J Biochem
Year2000
Volume267
Pages1100-9
AuthorsMay C, Hohne M, Gnau P, Schwennesen K, Kindl H
TitleThe N-terminal beta-barrel structure of lipid body lipoxygenase mediates its binding to liposomes and lipid bodies.
[39]
PubMed ID11029517
JournalInt J Mol Med
Year2000
Volume6
Pages521-6
AuthorsSkrzypczak-Jankun E, McCabe NP, Selman SH, Jankun J
TitleCurcumin inhibits lipoxygenase by binding to its central cavity: theoretical and X-ray evidence.
[40]
PubMed ID11396936
JournalBiochem Biophys Res Commun
Year2001
Volume284
Pages563-7
AuthorsKariapper MS, Dunham WR, Funk MO Jr
TitleIron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme.
[41]
PubMed ID11741336
JournalBiochem Biophys Res Commun
Year2001
Volume289
Pages1295-300
AuthorsMalvezzi-Campeggi F, Rosato N, Finazzi-Agro A, Maccarrone M
TitleEffect of denaturants on the structural properties of soybean lipoxygenase-1.
[42]
CommentsX-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
PubMed ID11412104
JournalBiochemistry
Year2001
Volume40
Pages7509-17
AuthorsTomchick DR, Phan P, Cymborowski M, Minor W, Holman TR
TitleStructural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1.
Related PDB1f8n,1fgm,1fgo,1fgq,1fgr,1fgt
Related Swiss-protP08170
[43]
PubMed ID11407646
JournalBiophys Chem
Year2001
Volume90
Pages303-6
AuthorsMaccarrone M, Bari M, Battista N, Finazzi-Agro A
TitleThe catalytic efficiency of soybean lipoxygenase-1 is enhanced at low gravity.
[44]
PubMed ID11321679
JournalBiophys Chem
Year2001
Volume90
Pages97-101
AuthorsMaccarrone M, Bari M, Battista N, Finazzi-Agro A
TitleThe catalytic efficiency of soybean lipoxygenase-1 is enhanced at low gravity.
[45]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed ID11686682
JournalJ Am Chem Soc
Year2001
Volume123
Pages10814-20
AuthorsSkrzypczak-Jankun E, Bross RA, Carroll RT, Dunham WR, Funk MO Jr
TitleThree-dimensional structure of a purple lipoxygenase.
Related PDB1ik3
Related Swiss-protP09186
[46]
PubMed ID12105957
JournalJ Agric Food Chem
Year2002
Volume50
Pages4270-4
AuthorsNoordermeer MA, Van Der Goot W, Van Kooij AJ, Veldsink JW, Veldink GA, Vliegenthart JF
TitleDevelopment of a biocatalytic process for the production of c6-aldehydes from vegetable oils by soybean lipoxygenase and recombinant hydroperoxide lyase.
[47]
PubMed ID11942823
JournalJ Am Chem Soc
Year2002
Volume124
Pages3865-74
AuthorsKnapp MJ, Rickert K, Klinman JP
TitleTemperature-dependent isotope effects in soybean lipoxygenase-1: correlating hydrogen tunneling with protein dynamics.
[48]
CommentsX-ray crystallography
PubMed ID12964012
JournalInt J Mol Med
Year2003
Volume12
Pages415-20
AuthorsSkrzypczak-Jankun E, Zhou K, Jankun J
TitleInhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead.
Related PDB1jnq
[49]
CommentsX-ray crystallography
PubMed ID12792803
JournalInt J Mol Med
Year2003
Volume12
Pages17-24
AuthorsSkrzypczak-Jankun E, Zhou K, McCabe NP, Selman SH, Jankun J
TitleStructure of curcumin in complex with lipoxygenase and its significance in cancer.
Related PDB1hu9
[50]
PubMed ID12626522
JournalJ Biol Chem
Year2003
Volume278
Pages18281-8
AuthorsDi Venere A, Salucci ML, van Zadelhoff G, Veldink G, Mei G, Rosato N, Finazzi-Agro A, Maccarrone M
TitleStructure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity.
[51]
CommentsX-ray crystallography
PubMed ID14993710
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages613-5
AuthorsSkrzypczak-Jankun E, Borbulevych OY, Jankun J
TitleSoybean lipoxygenase-3 in complex with 4-nitrocatechol.
Related PDB1no3
[52]
PubMed ID15125669
JournalJ Am Chem Soc
Year2004
Volume126
Pages5763-75
AuthorsHatcher E, Soudackov AV, Hammes-Schiffer S
TitleProton-coupled electron transfer in soybean lipoxygenase.
[53]
PubMed ID14971933
JournalJ Am Chem Soc
Year2004
Volume126
Pages2006-15
AuthorsVahedi-Faridi A, Brault PA, Shah P, Kim YW, Dunham WR, Funk MO Jr
TitleInteraction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition.
[54]
CommentsX-ray crystallography
PubMed ID14705020
JournalProteins
Year2004
Volume54
Pages13-9
AuthorsBorbulevych OY, Jankun J, Selman SH, Skrzypczak-Jankun E
TitleLipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution.
Related PDB1n8q


createdupdated
2004-11-222009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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