Literature summary for 1.8.3.2 extracted from

Faccio, G.; Kruus, K.; Buchert, J.; Saloheimo, M.
Secreted fungal sulfhydryl oxidases: Sequence analysis and characterisation of a representative flavin-dependent enzyme from Aspergillus oryzae (2010), BMC Biochem., 11, 31.

Search for more literature for 1.8.3.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Trichoderma reesei	Aspergillus oryzae

Inhibitors

Inhibitors	Comment	Organism	Structure
KI	1 mM, 65% residual activity	Aspergillus oryzae
MgSO4	1 mM, 55% residual activity	Aspergillus oryzae
Na2SO4	1 mM, 61% residual activity	Aspergillus oryzae
sodium dodecylsulfate	1 mM, 58% residual activity	Aspergillus oryzae
Urea	1 mM, 80% residual activity	Aspergillus oryzae
ZnSO4	1 mM, complete inhibition	Aspergillus oryzae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.55	-	D-Cys	pH 7.5, 20°C	Aspergillus oryzae
2.41	-	dithiothreitol	pH 7.5, 20°C	Aspergillus oryzae
2.78	-	glutathione	pH 7.5, 20°C	Aspergillus oryzae
6.11	-	L-Cys	pH 7.5, 20°C	Aspergillus oryzae
9.73	-	2-mercaptoethanol	pH 7.5, 20°C	Aspergillus oryzae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
43959	-	x * 45000, SDS-PAGE, x * 43959, mass spectrometry	Aspergillus oryzae
45000	-	x * 45000, SDS-PAGE, x * 43959, mass spectrometry	Aspergillus oryzae

Organism

Organism	UniProt	Comment	Textmining
Aspergillus oryzae	Q2UA33	-	-
Aspergillus oryzae ATCC 42149	Q2UA33	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da	Aspergillus oryzae

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Aspergillus oryzae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 2-mercaptoethanol + O2	-	Aspergillus oryzae	(ethyldisulfanyl)ethane + H2O2	-	?
2 2-mercaptoethanol + O2	-	Aspergillus oryzae ATCC 42149	(ethyldisulfanyl)ethane + H2O2	-	?
2 D-Cys + O2	-	Aspergillus oryzae	D-cystine + H2O2	-	?
2 D-Cys + O2	-	Aspergillus oryzae ATCC 42149	D-cystine + H2O2	-	?
2 dithiothreitol + O2	-	Aspergillus oryzae	dithiothreitol disulfide + H2O2	-	?
2 dithiothreitol + O2	-	Aspergillus oryzae ATCC 42149	dithiothreitol disulfide + H2O2	-	?
2 glutathione + O2	-	Aspergillus oryzae	glutathione disulfide + H2O2	-	?
2 glutathione + O2	-	Aspergillus oryzae ATCC 42149	glutathione disulfide + H2O2	-	?
2 L-Cys + O2	-	Aspergillus oryzae	L-cystine + H2O2	-	?
2 L-Cys + O2	-	Aspergillus oryzae ATCC 42149	L-cystine + H2O2	-	?

Subunits

Subunits	Comment	Organism
?	x * 45000, SDS-PAGE, x * 43959, mass spectrometry	Aspergillus oryzae

Synonyms

Synonyms	Comment	Organism
Sox1	-	Aspergillus oryzae

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
40	-	24 h, more than 70% of initial activity	Aspergillus oryzae
50	-	1 h, 40% of initial activity	Aspergillus oryzae
57	-	melting tepmerature	Aspergillus oryzae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
50	100	2-mercaptoethanol	pH 7.5, 20°C	Aspergillus oryzae
5950	-	D-Cys	pH 7.5, 20°C	Aspergillus oryzae
52300	-	L-Cys	pH 7.5, 20°C	Aspergillus oryzae
309000	-	dithiothreitol	pH 7.5, 20°C	Aspergillus oryzae
3600000	-	glutathione	pH 7.5, 20°C	Aspergillus oryzae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	-	Aspergillus oryzae

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
4	8	24 h, more than 80% of initial activity	Aspergillus oryzae

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
3840	-	D-Cys	pH 7.5, 20°C	Aspergillus oryzae
8560	-	L-Cys	pH 7.5, 20°C	Aspergillus oryzae
128000	-	dithiothreitol	pH 7.5, 20°C	Aspergillus oryzae
515000	-	2-mercaptoethanol	pH 7.5, 20°C	Aspergillus oryzae
1290000	-	glutathione	pH 7.5, 20°C	Aspergillus oryzae

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Release 2023.1 (January 2023)