EzCatDB: S00217

DB codeS00217
CATH domainDomain 13.20.20.70Catalytic domain
E.C.1.1.3.15
CSA1gox

CATH domainRelated DB codes (homologues)
3.20.20.70S00215,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
Swiss-protKEGG

P05414
Protein namePeroxisomal (S)-2-hydroxy-acid oxidase(S)-2-hydroxy-acid oxidase
glycolate oxidase
hydroxy-acid oxidase A
hydroxy-acid oxidase B
glycolate oxidase
oxidase, L-2-hydroxy acid
hydroxyacid oxidase A
L-alpha-hydroxy acid oxidase
L-2-hydroxy acid oxidase
SynonymsEC 1.1.3.15
Glycolate oxidase
GOX
Short chain alpha-hydroxy acid oxidase

KEGG pathways
MAP codePathways
MAP00630Glyoxylate and dicarboxylate metabolism

Swiss-prot:Accession NumberP05414
Entry nameGOX_SPIOL
Activity(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2).
SubunitHomotetramer or homooctamer.
Subcellular locationPeroxisome.
CofactorFMN.


CofactorsSubstratesProducts
KEGG-idC00061C00007C02613C00027C00161
CompoundFMNO2(S)-2-Hydroxy acidH2O22-Oxo acid
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionotherscarbohydrate,carboxyl groupotherscarbohydrate,carboxyl group
1al7ABound:FMNUnboundUnboundUnboundUnbound
1al8ABound:FMNUnboundUnboundUnboundUnbound
1goxABound:FMNUnboundUnboundUnboundUnbound
1gylABound:FMNUnboundUnboundUnboundUnbound
1gylBUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P05414
pdbCatalytic residuescomment
1al7ATYR 24;TYR 129;HIS 254;ARG 257

1al8ATYR 24;TYR 129;HIS 254;ARG 257

1goxATYR 24;TYR 129;HIS 254;ARG 257

1gylA      ;TYR 129;HIS 254;ARG 257
mutant Y24F
1gylB      ;TYR 129;HIS 254;ARG 257
mutant Y24F

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.3626-3627
[7]Scheme 1, Scheme 2, p.413-415
[11]Fig.6, p.1012-1014
[15]Fig.1, Fig.4

references
[1]
PubMed ID457688
JournalJ Biol Chem
Year1979
Volume254
Pages7403-4
AuthorsLindqvist Y, Branden CI
TitlePreliminary crystallographic data for glycolate oxidase from spinach.
[2]
PubMed ID7012375
JournalJ Mol Biol
Year1980
Volume143
Pages201-11
AuthorsLindqvist Y, Branden CI
TitleStructure of glycolate oxidase from spinach at a resolution of 5.5 A.
[3]
CommentsACTIVE SITE
Medline ID89123500
PubMed ID2644287
JournalJ Biol Chem
Year1989
Volume264
Pages3624-8
AuthorsLindqvist Y, Branden CI
TitleThe active site of spinach glycolate oxidase.
Related Swiss-protP05414
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID90040713
PubMed ID2681790
JournalJ Mol Biol
Year1989
Volume209
Pages151-66
AuthorsLindqvist Y
TitleRefined structure of spinach glycolate oxidase at 2 A resolution.
Related PDB1gox
Related Swiss-protP05414
[5]
PubMed ID8241149
JournalBiochemistry
Year1993
Volume32
Pages12959-67
AuthorsMitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA
TitleA novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida.
[6]
PubMed ID8348965
JournalFEBS Lett
Year1993
Volume327
Pages361-5
AuthorsSandalova T, Lindqvist Y
TitleCrystal structure of apo-glycolate oxidase.
[7]
CommentsX-ray crystallography
PubMed ID7705356
JournalEur J Biochem
Year1995
Volume228
Pages408-16
AuthorsStenberg K, Clausen T, Lindqvist Y, Macheroux P
TitleInvolvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase.
Related PDB1gyl
[8]
PubMed ID8566780
JournalGene
Year1995
Volume167
Pages215-9
AuthorsPayne MS, Petrillo KL, Gavagan JE, Wagner LW, DiCosimo R, Anton DL
TitleHigh-level production of spinach glycolate oxidase in the methylotrophic yeast Pichia pastoris: engineering a biocatalyst.
[9]
PubMed ID8987534
JournalAppl Microbiol Biotechnol
Year1996
Volume46
Pages46-54
AuthorsGellissen G, Piontek M, Dahlems U, Jenzelewski V, Gavagan JE, DiCosimo R, Anton DL, Janowicz ZA
TitleRecombinant Hansenula polymorpha as a biocatalyst: coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene.
[10]
PubMed ID9272859
JournalGene
Year1997
Volume194
Pages179-82
AuthorsPayne MS, Petrillo KL, Gavagan JE, DiCosimo R, Wagner LW, Anton DL
TitleEngineering Pichia pastoris for biocatalysis: co-production of two active enzymes.
[11]
CommentsX-ray crystallography
PubMed ID9144771
JournalProtein Sci
Year1997
Volume6
Pages1009-15
AuthorsStenberg K, Lindqvist Y
TitleThree-dimensional structures of glycolate oxidase with bound active-site inhibitors.
Related PDB1al7,1al8
[12]
PubMed ID10375564
JournalCurr Opin Plant Biol
Year1999
Volume2
Pages214-22
AuthorsDouce R, Neuburger M
TitleBiochemical dissection of photorespiration.
[13]
PubMed ID9891009
JournalJ Biol Chem
Year1999
Volume274
Pages2401-7
AuthorsKohler SA, Menotti E, Kuhn LC
TitleMolecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.
[14]
PubMed ID10850983
JournalJ Bacteriol
Year2000
Volume182
Pages3688-92
AuthorsGraupner M, Xu H, White RH
TitleIdentification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
[15]
PubMed ID10694883
JournalTrends Biochem Sci
Year2000
Volume25
Pages126-32
AuthorsFraaije MW, Mattevi A
TitleFlavoenzymes: diverse catalysts with recurrent features.

comments
According to the literature [3], this enzyme catalyzes the following reactions:
(A) Hydride transfer from FMN to hydroxy acid, giving FMNH2 and oxo acid:
(B) Hydride transfer from FMNH2 to O2, giving FMN and H2O2:

createdupdated
2004-07-152009-02-26


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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