Literature summary for 6.2.1.45 extracted from

Xie, S.T.
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1) (2014), Biosci. Biotechnol. Biochem., 78, 1542-1549.

Search for more literature for 6.2.1.45

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of N-terminally His6-tagged N-terminal domains of the enzyme, residues 1-439, in Escherichia coli strain BL21(DE3) from vector pETDuet-1	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant N-terminal enzyme domains comprising residues 1-439, hanging drop vapor diffusion method, mixing of 0.0015 ml of 15 mg/ml protein in 10mM Tris-HCl, pH 8.0, 150mM NaCl, and 2 mM DTT, with 0.0015 ml of reservoir solution containing 0.1 M Na3-citrate, pH 5.6, and 3.2 M NH4Ac, microseeding, 3 days, 21°C, X-ray diffraction structure determination and analysis at 2.75 A resolution	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
4[4-(5-nitro-furan-2-ylmethylene)-3,5-dioxo-pyrazolidin-1-yl]-benzoic acid ethyl ester	i.e. PYR-41	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine	Homo sapiens	-	AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22314	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged N-terminal enzyme domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, tag cleavage by 3C protease, another step of nickel affinity chromatography, followed by gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine	-	Homo sapiens	AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme N-terminal domains contain inactive adenylation domain (IAD) and the first catalytic cysteine half-domain (FCCH). The IAD domain covers from Met1 to Glu204 and Val295 to Ile439 and that the FCCH domain covers from Glu205 to Gln294. The structure of ubiquitin E1 consists of four different domain blocks, overview. The enzyme forms a pseudo-dimer	Homo sapiens

Synonyms

Synonyms	Comment	Organism
E1	-	Homo sapiens
Ubiquitin-activating enzyme	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	sequence and structure comparisons, overview	Homo sapiens
physiological function	ubiquitin-activating enzyme (E1) is a key regulator in protein ubiquitination, which lies on the upstream of the ubiquitin-related pathways and determines the activation of the downstream enzyme cascade	Homo sapiens

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Release 2023.1 (January 2023)