Literature summary for 3.4.19.15 extracted from

Cao, S.; Hepowit, N.; Maupin-Furlow, J.A.
Ubiquitin-like protein SAMP1 and JAMM/MPN+ metalloprotease HvJAMM1 constitute a system for reversible regulation of metabolic enzyme activity in archaea (2015), PLoS ONE, 10, e0128399.

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Organism

Organism	UniProt	Comment	Textmining
Haloferax volcanii	D4GTS4	-	-
Haloferax volcanii DSM 3757	D4GTS4	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N6-[SAMP1]-[MoaE]-L-lysine + H2O	MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1	Haloferax volcanii	[MoaE]-L-lysine + SAMP1	-	?
N6-[SAMP1]-[MoaE]-L-lysine + H2O	MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1	Haloferax volcanii DSM 3757	[MoaE]-L-lysine + SAMP1	-	?

General Information

General Information	Comment	Organism
physiological function	molybdopterin synthase activity is inhibited by covalent linkage of SAMP1 to the large subunit (MoaE) of MPT synthase. Metalloprotease JAMM1 cleaves the covalently linked inactive form of SAMP1-MoaE to the free functional individual SAMP1 and MoaE subunits of molybdopterin synthase	Haloferax volcanii

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Release 2023.1 (January 2023)