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

BRENDA support

Literature summary for 1.1.2.10 extracted from

  • Good, N.M.; Fellner, M.; Demirer, K.; Hu, J.; Hausinger, R.P.; Martinez-Gomez, N.C.
    Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function (2020), J. Biol. Chem., 295, 8272-8284 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Methylorubrum extorquens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of XoxF1, one with and another without pyrroloquinoline quinone, both with La3+x02 bound in the active-site region and coordinated by Asp320 Methylorubrum extorquens

Protein Variants

Protein Variants Comment Organism
D320A mutant enzyme does not bind La3+. Asp320 is needed for in vivo catalytic function, in vitro activity, and La3+x02 coordination Methylorubrum extorquens

Metals/Ions

Metals/Ions Comment Organism Structure
La3+ lanthanide-dependent enzyme Methylorubrum extorquens

Organism

Organism UniProt Comment Textmining
Methylorubrum extorquens C5B120
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methylorubrum extorquens

Synonyms

Synonyms Comment Organism
xoxF1
-
Methylorubrum extorquens

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone pyrroloquinoline quinone-containing enzyme Methylorubrum extorquens