Literature summary for 1.13.11.54 extracted from

Liu, X.; Garber, A.; Ryan, J.; Deshpande, A.; Ringe, D.; Pochapsky, T.C.
A model for the solution structure of human Fe(II)-bound acireductone dioxygenase and interactions with the regulatory domain of matrix metalloproteinase I (MMP-I) (2020), Biochemistry, 59, 4238-4249 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3)-CodonPlus-RIPL cells	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2	Homo sapiens	-	4-(methylsulfanyl)-2-oxobutanoate + formate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BV57	-	-

Purification (Commentary)

Purification (Comment)	Organism
Strep-Tactin resin column chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2	-	Homo sapiens	4-(methylsulfanyl)-2-oxobutanoate + formate	-	?

Synonyms

Synonyms	Comment	Organism
ARD	-	Homo sapiens
Fe(II)-bound acireductone dioxygenase	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the enzyme regulates the activity of matrix metalloproteinase I, which is involved in tumor metastasis, by binding the cytoplasmic transmembrane tail peptide of matrix metalloproteinase I	Homo sapiens

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Release 2023.1 (January 2023)