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Literature summary for 1.3.99.27 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
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Cloned(Commentary)

Cloned (Comment) Organism
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 Nonlabens dokdonensis

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.97 A resolution. CrtD structure is composed of an FAD-binding domain and a substrate-binding domain, which can be divided into two subdomains, a Rossmann fold-like subdomain and a lid subdomain. 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
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Nonlabens dokdonensis DSW-6 L7WC64
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Synonyms

Synonyms Comment Organism
CrtD
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 Nonlabens dokdonensis
DDD_2394
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 Nonlabens dokdonensis

Cofactor

Cofactor Comment Organism Structure
FAD the FAD-binding site is located at the G-x-G-x-x-G nucleotide-binding motif, comprising residues Gly8-Ala9-Gly10-Ile11-Gly12-Gly13 Nonlabens dokdonensis

General Information

General Information Comment Organism
physiological function CrtD is involved in the production of gamma-carotenoids by desaturating the C3'-C4'-position of 1'-OH-gamma-carotenoid Nonlabens dokdonensis