Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.1.3.15: (S)-2-hydroxy-acid oxidase

This is an abbreviated version!
For detailed information about (S)-2-hydroxy-acid oxidase, go to the full flat file.

Word Map on EC 1.1.3.15

Reaction

an (S)-2-hydroxy carboxylate
+
O2
=
a 2-oxo carboxylate
 +
H2O2

Synonyms

(L)-2-HAOX, (S)-2-hydroxy-acid oxidase, peroxisomal, 2-hydroxy acid oxidase, CSUB_C1080, EC 1.1.3.1, GLO, Glo1, GLO3, Glo4, glycolate oxidase, GO, GO1, GOX, GOX1, GOX2, HAO1, Hao2, HAOX, HAOX1, HAOX2, HAOX3, hydroxy-acid oxidase A, hydroxy-acid oxidase B, hydroxyacid oxidase 1, hydroxyacid oxidase A, L-2-hydroxy acid oxidase, L-2-hydroxyacid oxidase A, L-alpha-hydroxy acid oxidase, L-amino acid oxidase, L-LAC-OX, L-lactate monooxygenase, L-lactate oxidase, L-LOx, lactate oxidase, LCHAO, LctO, lHAOX1, lHAOX2, long chain hydroxy acid oxidase, long chain l-2-hydroxy acid oxidase, long chain L-2-hydroxy acid oxidase 2, long-chain 2-hydroxy acid oxidase, long-chain L-alpha-hydroxy acid oxidase, LOX, More, NbS00005125g0015, NbS00060838g0004, Nbv5tr6245008, Os03g0786100, Os04g0623500, Os07g0616500, oxidase, L-2-hydroxy acid, RCOM_0631490, RCOM_0684800

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.15 (S)-2-hydroxy-acid oxidase

Crystallization

Crystallization on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.0 A resolution, octamer with non-crystallographic two- and four-fold axes
-
hanging-drop or sitting-drop vapour diffusion method, 2.44 A resolution, large diffracting crystals of LOXR181M are obtained. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632 A, c= 200.263 A, alpha = beta = gamma =90°. There are four monomers in the asymmetric unit
-
resolution to 1.9 A. One pyruvate molecule is bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265
-
sitting-drop vapor diffusion technique. Crystal structure of wild-type enzyme at 2.1 A resolution. Space group I422 of unit-cell parameters a = b = 191.096 A, c = 194.497 A and alpha = beta = gamma = 90° with four monomers per asymmetric unit
-
sitting-drop vapour-diffusion method, determination of structure at 2.1 A resolution
-
unbound enzyme and in complex with D-lactate, both at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but an active site base, His265, flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement, creating a new hydrogen bonding network between His265-Asp174-Lys221 and, furthermore, brings molecular oxygen in between D-lactate and His265. In the mechanism of the subsequent oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide
-
structures of recombinant GO complexed with sulfate, glyoxylate, and 4-carboxy-5-dodecylsulfanyl-1,2,3-triazole (CDST), determined by X-ray crystallography are reported. A loop region (loop 4), is completely visible when the GO active site contains a small ligand. Lack of electron density for this loop in the GOCDST complex, mimicking a large substrate, indicates that a disordered to ordered transition occurs with substrate binding. Conformational flexibility of Trp110 is responsible for enabling GO to react with R-hydroxy acids. Movement of Trp110 disrupts a hydrogen-bonding network between Trp110, Leu191, Tyr134, and Tyr208. This loss indicates that active site movements are directly linked to changes in the conformation of loop 4
apo-GOX structure and its complex structure with cofactor FMN. The binding of FMN induces a pronounced conformational change of the GOX tetramer. A conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity
study of the nanomechanical properties of lactate oxidase monolayer immobilized on gold substrate by atomic force microscopy. The data fit by the Hertz model for a conical indenter, an average value of Young's modulus for the protein layer is in the 0.5-0.8 GPa range
-
analysis of the crystal structure of enzyme LCHAO in complex with cofactor FMN and inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole (CCPST) at 1.3 A resolution
sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4°C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution
ammonium sulfate precipitation, 2.6 A resolution of a two subunit apoenzyme
-
tert-butanol precipitation, bound active-site inhibitors
-