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Literature summary for 1.1.1.105 extracted from

  • Belyaeva, O.V.; Chetyrkin, S.V.; Kedishvili, N.Y.
    Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4 (2003), Chem. Biol. Interact., 143-144, 279-287.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTAM1-Y13 truncated RoDH-4 that lacks the first thirteen amino acids of the N-terminal segment is partially active and exhibits the apparent Km value for androsterone similar to that of the wild-type enzyme, truncated mutant behaves as an integral membrane protein Homo sapiens
DELTAS295-L317 removal of 23 N-terminal hydrophobic amino acids results in significant loss of activity and a 14fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein Homo sapiens
DELTAY291-L317 removal of the C-terminal 27 amino acid segment results in about 600fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein Homo sapiens
additional information protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane behaves as an integral membrane protein, RoDH-4 contains four potential membrane-spanning domains Homo sapiens 16020
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Organism

Organism UniProt Comment Textmining
Homo sapiens O75462
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
RoDH-4 RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
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Homo sapiens