DB code: S00217

CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
E.C. 1.1.3.15
CSA 1gox
M-CSA 1gox
MACiE

CATH domain Related DB codes (homologues)
3.20.20.70 : TIM Barrel S00215 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P05414 Peroxisomal (S)-2-hydroxy-acid oxidase
EC 1.1.3.15
Glycolate oxidase
GOX
Short chain alpha-hydroxy acid oxidase
PF01070 (FMN_dh)
[Graphical View]

KEGG enzyme name
(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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P05414 GOX_SPIOL (S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2). Homotetramer or homooctamer. Peroxisome. FMN.

KEGG Pathways
Map code Pathways E.C.
MAP00630 Glyoxylate and dicarboxylate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00061 C00007 C02613 C00027 C00161
E.C.
Compound FMN O2 (S)-2-Hydroxy acid H2O2 2-Oxo acid
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion others carbohydrate,carboxyl group others carbohydrate,carboxyl group
ChEBI 17621
17621
15379
26689
27140
15379
26689
27140
16240
16240
PubChem 643976
643976
977
977
22326046
784
22326046
784
1al7A Bound:FMN Unbound Unbound Unbound Unbound
1al8A Bound:FMN Unbound Unbound Unbound Unbound
1goxA Bound:FMN Unbound Unbound Unbound Unbound
1gylA Bound:FMN Unbound Unbound Unbound Unbound
1gylB Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P05414

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1al7A TYR 24;TYR 129;HIS 254;ARG 257
1al8A TYR 24;TYR 129;HIS 254;ARG 257
1goxA TYR 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
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 457688
Journal J Biol Chem
Year 1979
Volume 254
Pages 7403-4
Authors Lindqvist Y, Branden CI
Title Preliminary crystallographic data for glycolate oxidase from spinach.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7012375
Journal J Mol Biol
Year 1980
Volume 143
Pages 201-11
Authors Lindqvist Y, Branden CI
Title Structure of glycolate oxidase from spinach at a resolution of 5.5 A.
Related PDB
Related UniProtKB
[3]
Resource
Comments ACTIVE SITE
Medline ID 89123500
PubMed ID 2644287
Journal J Biol Chem
Year 1989
Volume 264
Pages 3624-8
Authors Lindqvist Y, Branden CI
Title The active site of spinach glycolate oxidase.
Related PDB
Related UniProtKB P05414
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 90040713
PubMed ID 2681790
Journal J Mol Biol
Year 1989
Volume 209
Pages 151-66
Authors Lindqvist Y
Title Refined structure of spinach glycolate oxidase at 2 A resolution.
Related PDB 1gox
Related UniProtKB P05414
[5]
Resource
Comments
Medline ID
PubMed ID 8241149
Journal Biochemistry
Year 1993
Volume 32
Pages 12959-67
Authors Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA
Title A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8348965
Journal FEBS Lett
Year 1993
Volume 327
Pages 361-5
Authors Sandalova T, Lindqvist Y
Title Crystal structure of apo-glycolate oxidase.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7705356
Journal Eur J Biochem
Year 1995
Volume 228
Pages 408-16
Authors Stenberg K, Clausen T, Lindqvist Y, Macheroux P
Title Involvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase.
Related PDB 1gyl
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8566780
Journal Gene
Year 1995
Volume 167
Pages 215-9
Authors Payne MS, Petrillo KL, Gavagan JE, Wagner LW, DiCosimo R, Anton DL
Title High-level production of spinach glycolate oxidase in the methylotrophic yeast Pichia pastoris: engineering a biocatalyst.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8987534
Journal Appl Microbiol Biotechnol
Year 1996
Volume 46
Pages 46-54
Authors Gellissen G, Piontek M, Dahlems U, Jenzelewski V, Gavagan JE, DiCosimo R, Anton DL, Janowicz ZA
Title Recombinant Hansenula polymorpha as a biocatalyst: coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9272859
Journal Gene
Year 1997
Volume 194
Pages 179-82
Authors Payne MS, Petrillo KL, Gavagan JE, DiCosimo R, Wagner LW, Anton DL
Title Engineering Pichia pastoris for biocatalysis: co-production of two active enzymes.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9144771
Journal Protein Sci
Year 1997
Volume 6
Pages 1009-15
Authors Stenberg K, Lindqvist Y
Title Three-dimensional structures of glycolate oxidase with bound active-site inhibitors.
Related PDB 1al7 1al8
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10375564
Journal Curr Opin Plant Biol
Year 1999
Volume 2
Pages 214-22
Authors Douce R, Neuburger M
Title Biochemical dissection of photorespiration.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9891009
Journal J Biol Chem
Year 1999
Volume 274
Pages 2401-7
Authors Kohler SA, Menotti E, Kuhn LC
Title Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 10850983
Journal J Bacteriol
Year 2000
Volume 182
Pages 3688-92
Authors Graupner M, Xu H, White RH
Title Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 10694883
Journal Trends Biochem Sci
Year 2000
Volume 25
Pages 126-32
Authors Fraaije MW, Mattevi A
Title Flavoenzymes: diverse catalysts with recurrent features.
Related PDB
Related UniProtKB

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:

Created Updated
2004-07-15 2009-02-26