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.

Reaction

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

Synonyms

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, 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-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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ENGINEERING
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