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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.3.2 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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Rattus norvegicus Q6IUU3
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.2 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 reaction mechanism Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.2 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 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
-
 ?
1.8.3.2 additional information redox cycling of the FAD moiety is essential for enzyme activity Rattus norvegicus ?
-
 ?
1.8.3.2 R-SH + O2
-
 Rattus norvegicus R-S-S-R + H2O2
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 ALRp
-
 Rattus norvegicus
1.8.3.2 sulfhydryl oxidase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 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