Literature summary for 4.4.1.16 extracted from

Heidenreich, T.; Wollers, S.; Mendel, R.R.; Bittner, F.
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration (2005), J. Biol. Chem., 280, 4213-4218.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.2	-	L-selenocysteine	pH 9.3, 37°C	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-selenocysteine + reduced acceptor	the NifS-like domain of molybdenum cofactor sulfurase ABA3 also exhibits selenocysteine lyase activity, although L-selenocysteine is unlikely to be a natural substrate	Arabidopsis thaliana	selenide + L-alanine + acceptor	-	?

Synonyms

Synonyms	Comment	Organism
ABA3-NifS	the NifS-like domain of molybdenum cofactor sulfurase ABA3 also exhibits selenocysteine lyase activity, although L-selenocysteine is unlikely to be a natural substrate	Arabidopsis thaliana

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Release 2023.1 (January 2023)