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Literature summary for 1.8.3.2 extracted from

  • Wu, C.K.; Dailey, T.A.; Dailey, H.A.; Wang, B.C.; Rose, J.P.
    The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase (2003), Protein Sci., 12, 1109-1118.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BC21 Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C62S site directed mutagenesis, inactive mutant, Cys62 is involved in redox cycling of the FAD moiety Rattus norvegicus
C62S/C65S site directed mutagenesis, inactive mutant, Cys62 and Cys65 are involved in redox cycling of the FAD moiety Rattus norvegicus
C65S site directed mutagenesis, inactive mutant, Cys65 is involved in redox cycling of the FAD moiety Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
R-SH + O2 Rattus norvegicus
-
R-S-S-R + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q6IUU3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by heat treatment, ethanol precipitation, ion exchange chromatography, and gel filtration Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 reaction mechanism Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dithiothreitol + O2 disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite Rattus norvegicus dithiothreitol disulfide + H2O2
-
?
additional information redox cycling of the FAD moiety is essential for enzyme activity Rattus norvegicus ?
-
?
R-SH + O2
-
Rattus norvegicus R-S-S-R + H2O2
-
?

Subunits

Subunits Comment Organism
dimer crystal structure, stabilization by extensive noncovalent interactions and a network of hydrogen bonds, structure fo the dimer interface Rattus norvegicus

Synonyms

Synonyms Comment Organism
ALRp
-
Rattus norvegicus
sulfhydryl oxidase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FAD dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity Rattus norvegicus