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

BRENDA support

Literature summary for 1.4.3.2 extracted from

  • Ju, Y.; Tong, S.; Gao, Y.; Zhao, W.; Liu, Q.; Gu, Q.; Xu, J.; Niu, L.; Teng, M.; Zhou, H.
    Crystal structure of a membrane-bound L-amino acid deaminase from Proteus vulgaris (2016), J. Struct. Biol., 195, 306-315.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Proteus vulgaris

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with flavin adenine dinucleotide. The overall fold is similar to D-amino acid oxidases with an additional hydrophobic insertion module on protein surface. The hydrophobic module serves as an extra membrane-binding site. Residues Q99 and R315 may interact with the carboxyl group of substrate amino acids, residues Q278 and L317 may be important for substrate selectivity Proteus vulgaris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Proteus vulgaris 16020
-

Organism

Organism UniProt Comment Textmining
Proteus vulgaris Q9LCB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information purified enzyme can generate a significant amount of hydrogen peroxide in vitro, it may be able to use dioxygen to directly reoxidize FADH2 Proteus vulgaris ?
-
?