Literature summary for 6.2.1.45 extracted from

Jaremko, M.; Jaremko, L.; Nowakowski, M.; Wojciechowski, M.; Szczepanowski, R.H.; Panecka, R.; Zhukov, I.; Bochtler, M.; Ejchart, A.
NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme (2014), J. Struct. Biol., 185, 69-78.

Crystallization (Commentary)

Crystallization (Comment)	Organism
NMR structural studies of the first catalytic cysteine half domain FCCH, interaction studies of FCCH and the other catalytic E1 domain SCCH, second catalytic cysteine half-domain. The E1 has several domains, an adenylation domain, composed of an active and inactive adenylation subdomains, and a catalytic cysteine domain, and smaller accessory domains: a four helix bundle and a ubiquitin fold domain. NMR cannot detect interactions between the FCCH and ubiquitin, or betweenween FCCH and SCCH if they are on separate poypeptide chains	Mus musculus

Crystallization (Comment)

Organism

NMR structural studies of the first catalytic cysteine half domain FCCH, interaction studies of FCCH and the other catalytic E1 domain SCCH, second catalytic cysteine half-domain. The E1 has several domains, an adenylation domain, composed of an active and inactive adenylation subdomains, and a catalytic cysteine domain, and smaller accessory domains: a four helix bundle and a ubiquitin fold domain. NMR cannot detect interactions between the FCCH and ubiquitin, or betweenween FCCH and SCCH if they are on separate poypeptide chains

Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Mus musculus	E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q02053	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine	E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex	Mus musculus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex	Mus musculus	?	-	?

Synonyms

Synonyms	Comment	Organism
ubiquitin-activating enzyme E1	-	Mus musculus