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Literature summary for 1.8.3.2 extracted from

  • Nivala, O.; Faccio, G.; Arvas, M.; Permi, P.; Buchert, J.; Kruus, K.; Mattinen, M.-L.
    Characterization of sulfhydryl oxidase from Aspergillus tubingensis (2017), BMC Biochem., 18, 15 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
zinc sulfate 10 mM, completely inhibited Aspergillus tubingensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.8
-
glutathione pH 7.4, 20°C Aspergillus tubingensis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aspergillus tubingensis
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
-
Aspergillus tubingensis

Organism

Organism UniProt Comment Textmining
Aspergillus tubingensis
-
-
-
Aspergillus tubingensis D-85248
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aspergillus tubingensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 D-cysteine + O2
-
Aspergillus tubingensis D-cystine + H2O2
-
?
2 D-cysteine + O2
-
Aspergillus tubingensis D-85248 D-cystine + H2O2
-
?
2 dithiothreitol + O2
-
Aspergillus tubingensis dithiothreitol disulfide + H2O2
-
?
2 dithiothreitol + O2
-
Aspergillus tubingensis D-85248 dithiothreitol disulfide + H2O2
-
?
2 glutathione + O2 the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol Aspergillus tubingensis glutathione disulfide + H2O2
-
?
2 glutathione + O2 the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol Aspergillus tubingensis D-85248 glutathione disulfide + H2O2
-
?
additional information peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme Aspergillus tubingensis ?
-
-
additional information peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme Aspergillus tubingensis D-85248 ?
-
-

Synonyms

Synonyms Comment Organism
AtSOX
-
Aspergillus tubingensis
sulfhydryl oxidase
-
Aspergillus tubingensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
the enzyme retains 89% of the initial activity after 20 h incubation Aspergillus tubingensis
50
-
the enzyme retains 75% of the initial activity after 20 h incubation Aspergillus tubingensis
60
-
the enzyme retains 18% of the initial activity after 20 h incubation Aspergillus tubingensis
70
-
the enzyme is inactivated within 15 min Aspergillus tubingensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Aspergillus tubingensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8.5 retains more than 80% of the initial activity in a pH range 4-8.5 within 20 h Aspergillus tubingensis

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme contains a non-covalently bound flavin cofactor Aspergillus tubingensis

General Information

General Information Comment Organism
evolution based on the analysis of 33 fungal genomes, sulfhydryl oxidase (SOX) encoding genes are close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, the enzyme (AtSOX) is evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin (GliT, HlmI and DepH) are evolutionary closely related to AtSOX whereas fungal thioreductases are more distant Aspergillus tubingensis
physiological function SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides Aspergillus tubingensis