 |
PDBsum entry 1bi9
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Aldehyde dehydrogenase
|
PDB id
|
|
|
|
1bi9
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structure of retinal dehydrogenase type ii at 2.7 a resolution: implications for retinal specificity.
|
|
|
Authors
|
|
A.L.Lamb,
M.E.Newcomer.
|
|
|
Ref.
|
|
Biochemistry, 1999,
38,
6003-6011.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Retinoic acid, a hormonally active form of vitamin A, is produced in vivo in a
two step process: retinol is oxidized to retinal and retinal is oxidized to
retinoic acid. Retinal dehydrogenase type II (RalDH2) catalyzes this last step
in the production of retinoic acid in the early embryo, possibly producing this
putative morphogen to initiate pattern formation. The enzyme is also found in
the adult animal, where it is expressed in the testis, lung, and brain among
other tissues. The crystal structure of retinal dehydrogenase type II
cocrystallized with nicotinamide adenine dinucleotide (NAD) has been determined
at 2.7 A resolution. The structure was solved by molecular replacement using the
crystal structure of a mitochondrial aldehyde dehydrogenase (ALDH2) as a model.
Unlike what has been described for the structures of two aldehyde dehydrogenases
involved in the metabolism of acetaldehyde, the substrate access channel is not
a preformed cavity into which acetaldehyde can readily diffuse. Retinal
dehydrogenase appears to utilize a disordered loop in the substrate access
channel to discriminate between retinaldehyde and short-chain aldehydes.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Purification, Crystallization and preliminary X-Ray diffraction studies of retinal dehydrogenase type ii.
|
|
|
Authors
|
|
A.L.Lamb,
X.Wang,
J.L.Napoli,
M.E.Newcomer.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 1998,
54,
639-642.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Restricted expression and retinoic acid-Induced downregulation of the retinaldehyde dehydrogenase type 2 (raldh-2) gene during mouse development.
|
|
|
Authors
|
|
K.Niederreither,
P.Mccaffery,
U.C.Dräger,
P.Chambon,
P.Dollé.
|
|
|
Ref.
|
|
Mech Dev, 1997,
62,
67-78.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Cloning of a cdna encoding an aldehyde dehydrogenase and its expression in escherichia coli. Recognition of retinal as substrate.
|
|
|
Authors
|
|
X.Wang,
P.Penzes,
J.L.Napoli.
|
|
|
Ref.
|
|
J Biol Chem, 1996,
271,
16288-16293.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 4.
Fig. 4. Rates of RA synthesis catalyzed by RalDH(II) versus
substrate concentrations. The rate of RA synthesis from retinal
(upper panel) or CRBP-retinal (lower panel) was measured with
the longer recombinant RalDH(II) translation product,
RalDH(II)/rL. In the lower panel, the molar ratio of total CRBP
to retinal was 2 at each concentration of retinal. Data were fit
with the nonlinear regression analysis program Enzfitter (43).
|
|
Figure 5.
Fig. 5. Synthesis of RA from retinal produced in situ by
microsomes and holo-CRBP. RalDH(II)/rL was titrated into a
mixture containing microsomes, holo-CRBP, apo-CRBP, NAD, and
NADP, and the incubation was done as described in the legend to
Table II.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from the ASBMB
|
|
|
|
|
|
|
