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

BRENDA support

Literature summary for 1.3.99.37 extracted from

  • Ahn, J.W.; Kim, K.J.
    Crystal structure of 1-OH-carotenoid 3,4-desaturase from Nonlabens dokdonensis DSW-6 (2015), Enzyme Microb. Technol., 77, 29-37.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Nonlabens dokdonensis

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.97 A resolution. Structure is composed of two distinct domains, an FAD-binding domain and a substrate-binding domain. The substrate-binding domain constitutes a long and hydrophobic tunnel with a length of about 40 A. The tunnel provides an appropriate substrate-binding site for the carotenoid such as 1'-OH-gamma-carotene with a length of about 35 A Nonlabens dokdonensis

Organism

Organism UniProt Comment Textmining
Nonlabens dokdonensis L7WC64
-
-
Nonlabens dokdonensis DSW-6 L7WC64
-
-

Synonyms

Synonyms Comment Organism
DDD_2394
-
Nonlabens dokdonensis
gamma-carotene desaturase
-
Nonlabens dokdonensis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Nonlabens dokdonensis