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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.45 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)

EC Number Crystallization (Comment) Organism
6.2.1.45 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

EC Number Inhibitors Comment Organism Structure
6.2.1.45 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

EC Number Metals/Ions Comment Organism Structure
6.2.1.45 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.45 Homo sapiens P22314
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.45 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)

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

Subunits

EC Number Subunits Comment Organism
6.2.1.45 additional information 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

EC Number Synonyms Comment Organism
6.2.1.45 E1
-
 Homo sapiens
6.2.1.45 Ubiquitin-activating enzyme
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.45 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
6.2.1.45 additional information sequence and structure comparisons, overview Homo sapiens
6.2.1.45 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