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1.1.1.105: all-trans-retinol dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about all-trans-retinol dehydrogenase (NAD+), go to the full flat file.

Word Map on EC 1.1.1.105

Reaction

all-trans-retinol-[cellular-retinol-binding-protein]
+
NAD+
=
all-trans-retinal-[cellular-retinol-binding-protein]
+
NADH
+
H+

Synonyms

ADH, alcohol dehydrogenase, all-trans retinol dehydrogenase, all-trans-retinol dehydrogenase, dehydrogenase, retinol, DHRS9, epidermal retinol dehydrogenase 2, LOC100185899, MDR, microsomal retinol dehydrogenase, mRDH1, NAD+-dependent retinoid-active short-chain dehydrogenase/reductase, P32, PDHC, photoreceptor retinol dehydrogenase isoform C, RDH-E2, RDH-like SDR, Rdh1, RDH10, RDH10a, RDH10b, RDH10c, RDH12, RDH16, RDH2, RDH7, RDH8, RDHE2, RDHE2S, RDHL, retinal reductase, retinene reductase, retinoid dehydrogenase/reductase, retinol dehydrogenase (vitamin A1), retinol dehydrogenase 10, retinol dehydrogenase 12, retinol dehydrogenase 2, retinol dehydrogenase 4, retinol dehydrogenase epidermal 2, retinol dehydrogenase epidermal 2-similar, RL-HSD, RoDH-4, RoDH-like 3alpha-hydroxysteroid dehydrogenase, RoDH4, SDR16C5, SDR16C6, XP_2120364

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.105 all-trans-retinol dehydrogenase (NAD+)

Engineering

Engineering on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C201R
the loss of function mutant is associated with severe loss of retinal functionand early onset severe retinal dystrophy
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
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
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
G43A/G47A/G49A
the triple mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214R
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169D
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197A
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197C
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197G
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197T
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197V
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210F
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
L3R/L5R/R16Q/R19Q/R21Q
-
RDH1 mutant, deleting the positive charges from the C-terminal end of the leader, and inserting two arginine residues near the N-terminus of the signaling sequence causes 95% inversion from cytoplasmic to luminal, the mutant faces the lumen
additional information