PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14551196-6 2004 We find that disrupting alrA, the gene encoding aldehyde reductase, results in the loss of alrA mRNA and AlrA protein and a decrease in the ability of cell lysates to reduce both glyceraldehyde and glucose in an NADPH-coupled reaction. NADP 212-217 aldo-keto reductase family 1 member A1 Homo sapiens 48-66 15720144-8 2005 The competing activation of BP-7,8-diol by P450 1A1/P450 1B1 and AKR1A1 was studied with varied NADPH:NAD+ ratios. NADP 96-101 aldo-keto reductase family 1 member A1 Homo sapiens 65-71 18402469-6 2008 P450 and AKR enzymes equally competed for (+/-)-B[ a]P-7,8-diol substrate at an NADPH/NAD (+) ratio equal to 0.001. NADP 80-85 aldo-keto reductase family 1 member A1 Homo sapiens 9-12 16245351-0 2006 Exploitation of the alcohol dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid. NADP 50-54 aldo-keto reductase family 1 member A1 Homo sapiens 20-41 16245351-1 2006 The performance of a new NADP-regeneration system, based on the use of alcohol dehydrogenase (ADH)-acetone, has been investigated for the regioselective oxidation of cholic acid (1) to 12-ketochenodeoxycholic acid (2). NADP 25-29 aldo-keto reductase family 1 member A1 Homo sapiens 71-92 16245351-1 2006 The performance of a new NADP-regeneration system, based on the use of alcohol dehydrogenase (ADH)-acetone, has been investigated for the regioselective oxidation of cholic acid (1) to 12-ketochenodeoxycholic acid (2). NADP 25-29 aldo-keto reductase family 1 member A1 Homo sapiens 94-97 10706394-3 2000 AR and AHR activity were expressed as the area under the peak obtained by post-column spectrophotometric detection of the decrease of coenzyme (NADPH) in each enzyme reaction. NADP 144-149 aldo-keto reductase family 1 member A1 Homo sapiens 7-10 12585477-5 2003 The ISFET devices functionalized with the NADH and NADPH membranes are employed in the analysis of the biocatalyzed oxidation of lactic acid and ethanol in the presence of lactate dehydrogenase and alcohol dehydrogenase, respectively. NADP 51-56 aldo-keto reductase family 1 member A1 Homo sapiens 198-219 7669785-13 1995 The mode of inhibition of aldehyde reductase by aldose reductase inhibitors (ARIs) is generally similar to that of aldose reductase and involves binding to the E:NADP+ complex, as shown by kinetic and direct inhibitor-binding experiments. NADP 162-167 aldo-keto reductase family 1 member A1 Homo sapiens 26-44 10493777-2 1999 METHODS: The crystal structure of porcine aldehyde reductase in complex with NADPH and the aldose reductase inhibitor sorbinil was determined. NADP 77-82 aldo-keto reductase family 1 member A1 Homo sapiens 42-60 9675019-1 1998 The only major structural difference between aldehyde reductase, a primarily NADPH-dependent aldo-keto reductase, and aldose reductase, a dually coenzyme-specific (NADPH/NADH) member of the same superfamily, is an additional eight amino acid residues in the substrate/inhibitor binding site (C-terminal region) of aldehyde reductase. NADP 77-82 aldo-keto reductase family 1 member A1 Homo sapiens 45-63 14340079-0 1965 THE ACTIVITY OF LIVER ALCOHOL DEHYDROGENASE WITH NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE AS COENZYME. NADP 49-92 aldo-keto reductase family 1 member A1 Homo sapiens 22-43 7552731-4 1995 Unlike aldose reductase, the N epsilon 2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH. NADP 181-186 aldo-keto reductase family 1 member A1 Homo sapiens 77-95 15299849-1 1995 Porcine aldehyde reductase-NADPH binary complex has been crystallized from a buffered ammonium sulfate solution. NADP 27-32 aldo-keto reductase family 1 member A1 Homo sapiens 8-26 15299849-5 1995 The aldehyde reductase-NADPH complex model is supported by electron density corresponding to NADPH not included in the search model. NADP 23-28 aldo-keto reductase family 1 member A1 Homo sapiens 4-22 15299849-5 1995 The aldehyde reductase-NADPH complex model is supported by electron density corresponding to NADPH not included in the search model. NADP 93-98 aldo-keto reductase family 1 member A1 Homo sapiens 4-22 15299849-7 1995 The structure of aldehyde reductase-NADPH binary complex will help clarify the mechanism of action for this enzyme and will lead to the development of pharmacologic agents to delay or prevent diabetic complications. NADP 36-41 aldo-keto reductase family 1 member A1 Homo sapiens 17-35 1815509-3 1991 Aldose reductase activity is expressed with either NADH or NADPH as cofactor, whereas aldehyde reductase utilizes only NADPH. NADP 119-124 aldo-keto reductase family 1 member A1 Homo sapiens 86-104 3890832-1 1985 Initial-rate studies of the low-Km aldehyde reductase-catalysed reduction of pyridine-3-aldehyde by NADPH gave families of parallel double-reciprocal plots, consistent with a double-displacement mechanism being obeyed. NADP 100-105 aldo-keto reductase family 1 member A1 Homo sapiens 35-53 7552731-1 1995 Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. NADP 83-88 aldo-keto reductase family 1 member A1 Homo sapiens 0-18 7552731-2 1995 The structure of porcine aldehyde reductase-NADPH binary complex has been determined by x-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 A resolution. NADP 44-49 aldo-keto reductase family 1 member A1 Homo sapiens 25-43 8032149-4 1994 Although H. pylori ADH was capable of utilizing both NADP and NAD as cofactors in alcohol oxidation, it showed a strong preference for NADP over NAD. NADP 53-57 aldo-keto reductase family 1 member A1 Homo sapiens 19-22 8032149-4 1994 Although H. pylori ADH was capable of utilizing both NADP and NAD as cofactors in alcohol oxidation, it showed a strong preference for NADP over NAD. NADP 135-139 aldo-keto reductase family 1 member A1 Homo sapiens 19-22 1901806-8 1991 Aldose reductase utilized both NADPH and NADH as coenzymes, whereas aldehyde reductase only NADPH. NADP 92-97 aldo-keto reductase family 1 member A1 Homo sapiens 68-86 2316395-4 1990 Various NAD(P)-dependent enzymes, sorbitol dehydrogenase, alcohol dehydrogenase and malate dehydrogenase, were co-immobilized on preactivated polyamide membranes with the bacterial system and used for the microdetermination of sorbitol, ethanol and oxaloacetate at the nanomolar level with a good precision. NADP 8-14 aldo-keto reductase family 1 member A1 Homo sapiens 58-79 2498333-2 1989 Aldehyde reductase [EC 1.1.1.2] and aldose reductase [EC 1.1.1.21] are monomeric NADPH-dependent oxidoreductases having wide substrate specificities for carbonyl compounds. NADP 81-86 aldo-keto reductase family 1 member A1 Homo sapiens 0-18 3435455-1 1987 Hepatic microsomal fractions from ADH (alcohol dehydrogenase)-negative deermice incubated with an NADPH-generating system metabolized butanol and ethanol at rates around 10 nmol/min per mg. NADP 98-103 aldo-keto reductase family 1 member A1 Homo sapiens 34-37 3435455-1 1987 Hepatic microsomal fractions from ADH (alcohol dehydrogenase)-negative deermice incubated with an NADPH-generating system metabolized butanol and ethanol at rates around 10 nmol/min per mg. NADP 98-103 aldo-keto reductase family 1 member A1 Homo sapiens 39-60 4399579-0 1971 Decreased thermal stability of alcohol dehydrogenase in the presence of oxidized nicotinamide-adenine dinucleotide or oxidized nicotinamide-adenine dinucleotide phosphate. NADP 127-170 aldo-keto reductase family 1 member A1 Homo sapiens 31-52 14340079-5 1965 The activity of pure crystalline liver alcohol dehydrogenase with NADP as coenzyme has been confirmed. NADP 66-70 aldo-keto reductase family 1 member A1 Homo sapiens 39-60 31649033-5 2019 Here, we de novo purified NADPH-coupled GSNOR activity from mammalian tissues and identified aldo-keto reductase family 1 member A1 (AKR1A1), the archetypal mammalian SNO-CoA reductase, as a primary mediator of NADPH-coupled GSNOR activity in these tissues. NADP 211-216 aldo-keto reductase family 1 member A1 Homo sapiens 93-131 31649033-5 2019 Here, we de novo purified NADPH-coupled GSNOR activity from mammalian tissues and identified aldo-keto reductase family 1 member A1 (AKR1A1), the archetypal mammalian SNO-CoA reductase, as a primary mediator of NADPH-coupled GSNOR activity in these tissues. NADP 211-216 aldo-keto reductase family 1 member A1 Homo sapiens 133-139 25256836-3 2014 A high Km aldehyde reductase has previously been reported to catalyse the NADP-dependent oxidation of GHB at high concentrations. NADP 74-78 aldo-keto reductase family 1 member A1 Homo sapiens 10-28 25256836-8 2014 Demolishing AKR1A1 expression in HepG2 cells leads to significant 82% decrease in NADP-dependent GHB-dehydrogenase activity at high concentration (10mM) of GHB. NADP 82-86 aldo-keto reductase family 1 member A1 Homo sapiens 12-18 20173089-5 2010 Formation of M4 and M5 was catalyzed by NADPH-dependent hepatic cytosolic enzymes, which were identified using selective chemical inhibitors (10 and 100 microM) for aldo-keto reductase (AKR) isoforms, short-chain dehydrogenase/reductase including carbonyl reductase, alcohol dehydrogenase, and quinone oxidoreductase. NADP 40-45 aldo-keto reductase family 1 member A1 Homo sapiens 267-288 20036445-1 2010 The structure of aldehyde reductase (ALR1) in ternary complex with the coenzyme NADPH and [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid (CMD), a potent inhibitor of aldose reductase (ALR2), was determined at 1.99A resolution. NADP 80-85 aldo-keto reductase family 1 member A1 Homo sapiens 17-35 31649033-5 2019 Here, we de novo purified NADPH-coupled GSNOR activity from mammalian tissues and identified aldo-keto reductase family 1 member A1 (AKR1A1), the archetypal mammalian SNO-CoA reductase, as a primary mediator of NADPH-coupled GSNOR activity in these tissues. NADP 26-31 aldo-keto reductase family 1 member A1 Homo sapiens 93-131 31649033-5 2019 Here, we de novo purified NADPH-coupled GSNOR activity from mammalian tissues and identified aldo-keto reductase family 1 member A1 (AKR1A1), the archetypal mammalian SNO-CoA reductase, as a primary mediator of NADPH-coupled GSNOR activity in these tissues. NADP 26-31 aldo-keto reductase family 1 member A1 Homo sapiens 133-139 27595938-4 2016 Using the differential scanning fluorimetry and the circular dichroism varying the urea concentration and temperature, we found that when the coenzyme NADP+ was absent, inhibitors such as isolithocholic acid stabilized the aldo-keto reductase AKR1A1 upon binding, which showed actually the three-state folding, but destabilized AKR1B10. NADP 151-156 aldo-keto reductase family 1 member A1 Homo sapiens 243-249 27595938-5 2016 In contrast, in the presence of NADP+ , they destabilized AKR1A1 and stabilized AKR1B10. NADP 32-37 aldo-keto reductase family 1 member A1 Homo sapiens 58-64 21276435-5 2011 Aldehyde reductase activity was examined in silenced cells by following the aldehyde-dependent conversion of NADPH to NADP at 340 nm. NADP 109-114 aldo-keto reductase family 1 member A1 Homo sapiens 0-18 21276435-5 2011 Aldehyde reductase activity was examined in silenced cells by following the aldehyde-dependent conversion of NADPH to NADP at 340 nm. NADP 109-113 aldo-keto reductase family 1 member A1 Homo sapiens 0-18