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

BRENDA support

1.8.3.2: thiol oxidase

This is an abbreviated version!
For detailed information about thiol oxidase, go to the full flat file.

Word Map on EC 1.8.3.2

Reaction

2 R'C(R)SH +

O2
=
R'C(R)S-S(R)CR'
+
H2O2

Synonyms

Ac92, AcMNPV P33, ALR, ALRp, AtSOX, augmenter of liver regeneration, DTT-oxidase, E10R, egg white oxidase, Ero1, Ero1p, ERV/ALR sulfhydryl oxidase, Erv1, Erv1p, Erv2, ERv2p, FAD-linked sulfhydryl oxidase, FAD-linked sulfhydryl oxidase ALR, FAD-sulfhydryl oxidase, flavin adenine dinucleotide-linked sulfhydryl oxidase, flavin-dependent sulfhydryl oxidase, GmQSOX1, GmQSOX2, hepatic regenerative stimulator substance, hepatopoietin, mitochondrial FAD-linked sulfhydryl oxidase ERV1, More, neuroblastoma-derived sulfhydryl oxidase, oxidase, thiol, P33, pB119L, protein pB119L, QSCN6, QSOX, QSOx1, QSOX1b, QSOX2, QSOX3, Quiescin Q6, quiescin Q6 sulfhydryl oxidase, quiescin Q6 sulfhydryl oxidase 1, quiescin Q6/sulfhydryl oxidase, quiescin sulfhydryl oxidase, quiescin sulfhydryl oxidase 1, quiescin sulhydryl oxidase, quiescin-like flavin-dependent sulfhydryl oxidase, Quiescin-sulfhydryl oxidase, quiescin/sulfhydryl oxidase, quiescin/sulfhydryl oxidase 1b, quiescin/sulphydryl oxidase, rQSOX, sfALR, SOX, Sox1, Sox2, SOXN, sulfhydryl oxidase, sulfhydryl oxidase SOx-3, sulfhydryl oxidase, P33, sulphydryl oxidase, thiol oxidase Erv1, thiooxidase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.3 With oxygen as acceptor
                1.8.3.2 thiol oxidase

Crystallization

Crystallization on EC 1.8.3.2 - thiol oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified unlabeled and selenomethionine-labeled pB119L-DELTAC, the protein crystallizes readily under a wide range of conditions, multiple anomalous dispersion, X-ray diffraction structure determination and analysis at 1.9 A resolution
crystal structure to 0.98 A resolution shows a configuration of the active-site cysteine residues and bound cofactor similar to that observed in other Erv sulfhydryl oxidases. Protein has a complex quaternary structural arrangement comprising a dimer of pseudodimers with a striking 40-degree kink in the interface helix between subunits
vapor diffusion sitting drops method at 16°C
partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv family enzymes. One pseudo-dimer subunit has lost its cofactor and catalytic activity
purified recombinant liver enzyme, native enzyme and selenomethionine enzyme, the latter is produced by microseeding with native enzyme, X-ray diffraction structure determination and analysis at 1.8 A resolution
crystal structures at 2.0 A resolution of the C-terminal domain and at 3.0 A resolution of a C30S/C133S double mutant. The C-terminal domain exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The N-terminal domain is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the N-terminal domain to the C-terminal domain of another subunit. The four-helix bundle of the C-terminal domain forms a wide platform for the electron donor N-terminal domain. Moreover,the amphipathic helix close to the shuttle redox enter may be critical for the recognition of Mia40, the upstream electron donor
Erv2p, X-ray diffraction structure determination and analysis
-
TbQSOX crystal structure analysis, PDB ID 3QD9
-