Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.17 extracted from

  • Schubert, H.L.; Hill, C.P.
    Structure of ATP-bound human ATP:cobalamin adenosyltransferase (2006), Biochemistry, 45, 15188-15196.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information enzyme mutations at residues Gly97, Ser174, Arg186, Arg190, Arg191, Glu193, and Gln234 can result in the metabolic disorder known as methylmalonic aciduria, MMA, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion Arg19 in the mitochondrial targeting sequence is important Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96EY8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA Homo sapiens ?
-
?
additional information only two of the three active sites within the trimer contain the bound ATP substrate, twenty residues at the enzyme’s N-terminus become ordered upon binding of ATP to form an ATP-binding site and an extended cleft that likely binds cobalamin, cobalamin binding site structure involving residue R186, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
trimer the enzyme forms a tightly associated trimer, where the monomer comprises a five-helix bundle and the active sites lie on the subunit interfaces, invariant residues and their function within the ATR structure, detailed overview Homo sapiens

Synonyms

Synonyms Comment Organism
ATP:cobalamin adenosyltransferase
-
Homo sapiens
ATR
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP twenty residues at the enzyme’s N-terminus become ordered upon binding of ATP to form an ATP-binding site, structure, overview Homo sapiens