Zobrazeno 1 - 10
of 81
pro vyhledávání: '"T G, Flynn"'
Publikováno v:
Chemico-Biological Interactions. :651-658
In order to understand more fully the structural features of aldo-keto reductases (AKRs) that determine their substrate specificities it would be desirable to obtain crystal structures of an AKR with a substrate at the active site. Unfortunately the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8b832f5429d744a8f7415a63c988f55
https://doi.org/10.1016/s0009-2797(00)00256-8
https://doi.org/10.1016/s0009-2797(00)00256-8
Publikováno v:
American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 274:R255-R261
Atrial natriuretic peptide (ANP), a peptide hormone produced by the heart, exerts a chronic hypotensive effect. Knockout mice with a homozygous disruption of the pro-ANP gene (−/−) are incapable of producing ANP and are hypertensive relative to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a80d39794283960b4cac376b94a2a250
https://doi.org/10.1152/ajpregu.1998.274.1.r255
https://doi.org/10.1152/ajpregu.1998.274.1.r255
Publikováno v:
Biochemical Pharmacology. 54:639-647
The aldo-keto reductases (AKRs) represent a growing oxidoreductase superfamily. Forty proteins have been identified and characterized as AKRs, and an additional fourteen genes may encode proteins related to the superfamily. Found in eukaryotes and pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b24623fc4fb760744bb5cd322f6603c
https://doi.org/10.1016/s0006-2952(97)84253-0
https://doi.org/10.1016/s0006-2952(97)84253-0
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 51:605-608
Porcine aldehyde reductase-NADPH binary complex has been crystallized from a buffered ammonium sulfate solution. The crystal form is hexagonal, space group P6{sub 5}22, with a = b = 67.2, c = 243.7 A, {alpha} = {beta} = 90.0 and {gamma} = 120.0 degre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b4204a655dcde4085c2b4c4dc208630
https://doi.org/10.1107/s0907444994013995
https://doi.org/10.1107/s0907444994013995
Autor:
Terrance J. Kubiseski, T G Flynn
Publikováno v:
Journal of Biological Chemistry. 270:16911-16917
Aldose reductase (ALR2) shows a strong specificity for its nucleotide coenzyme, binding NADPH much more tightly than NADH (KD of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f41c62509bad9b6045ae3601d9fac81
https://doi.org/10.1074/jbc.270.28.16911
https://doi.org/10.1074/jbc.270.28.16911
Publikováno v:
Gene. 158:275-280
The 13.2-kDa subunit of NADH:ubiquinone oxidoreductase has been shown to be an integral part of the bovine iron-sulfur (IP) part of the protein. This subunit has been shown to interact with at least two other protein subunits of the IP fragment. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ed5edcd5601c2f505787e6bd76f7b4e
https://doi.org/10.1016/0378-1119(95)00029-6
https://doi.org/10.1016/0378-1119(95)00029-6
Publikováno v:
Journal of Biological Chemistry. 269:2183-2188
Reaction of pig muscle aldose reductase with phenylglyoxal resulted in the chemical modification of 2 arginine residues with accompanying loss of catalytic activity. The amino acid sequences of radioactive peptides resulting from the reaction of aldo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a90f56767a8cc74ea786586cb9fb73a9
https://doi.org/10.1016/s0021-9258(17)42152-1
https://doi.org/10.1016/s0021-9258(17)42152-1
Publikováno v:
Journal of Biological Chemistry. 267:18953-18960
The zero-length cross-link between the inhibitory epsilon subunit and one of three catalytic beta subunits of Escherichia coli F1-ATPase (alpha 3 beta 3 gamma delta epsilon), induced by a water-soluble carbodiimide, 1-ethyl-3-[(3-dimethylamino) propy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1671a9e4c16b8785d794980203e4ceeb
https://doi.org/10.1016/s0021-9258(19)37053-x
https://doi.org/10.1016/s0021-9258(19)37053-x
Publikováno v:
Journal of Biological Chemistry. 267:6510-6517
Steady state kinetic analysis at pH 7.0 of the reduction of DL-glyceraldehyde by pig muscle aldose reductase showed that the enzyme follows a sequential ordered mechanism with NADPH binding first. However, the "off constant" for NADP+ in the forward
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6f0b3ba9db120478e63ba2731995a52
https://doi.org/10.1016/s0021-9258(19)50457-4
https://doi.org/10.1016/s0021-9258(19)50457-4
Publikováno v:
Journal of Biological Chemistry. 266:13028-13034
Amino acid sequencing of glucose 6-phosphate dehydrogenase (Glc6PD) from Leuconostoc mesenteroides yielded sequence for over 75% of the protein. Two oligonucleotides based on the amino acid sequence were used to isolate a partial Glc6PD gene clone (p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79af9b8568d5be2de4ad297a4610a924
https://doi.org/10.1016/s0021-9258(18)98798-3
https://doi.org/10.1016/s0021-9258(18)98798-3