Relevant bibliographies by topics / NADP-bound; NAD-bound

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Academic literature on the topic 'NADP-bound; NAD-bound'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "NADP-bound; NAD-bound"

1

Anderlund, Mikael, Torben L. Nissen, Jens Nielsen, John Villadsen, Jan Rydström, Bärbel Hahn-Hägerdal, and Morten C. Kielland-Brandt. "Expression of the Escherichia coli pntA andpntB Genes, Encoding Nicotinamide Nucleotide Transhydrogenase, in Saccharomyces cerevisiae and Its Effect on Product Formation during Anaerobic Glucose Fermentation." Applied and Environmental Microbiology 65, no. 6 (June 1, 1999): 2333–40. http://dx.doi.org/10.1128/aem.65.6.2333-2340.1999.

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ABSTRACT We studied the physiological effect of the interconversion between the NAD(H) and NADP(H) coenzyme systems in recombinantSaccharomyces cerevisiae expressing the membrane-bound transhydrogenase from Escherichia coli. Our objective was to determine if the membrane-bound transhydrogenase could work in reoxidation of NADH to NAD+ in S. cerevisiaeand thereby reduce glycerol formation during anaerobic fermentation. Membranes isolated from the recombinant strains exhibited reduction of 3-acetylpyridine-NAD+ by NADPH and by NADH in the presence of NADP+, which demonstrated that an active enzyme was present. Unlike the situation in E. coli, however, most of the transhydrogenase activity was not present in the yeast plasma membrane; rather, the enzyme appeared to remain localized in the membrane of the endoplasmic reticulum. During anaerobic glucose fermentation we observed an increase in the formation of 2-oxoglutarate, glycerol, and acetic acid in a strain expressing a high level of transhydrogenase, which indicated that increased NADPH consumption and NADH production occurred. The intracellular concentrations of NADH, NAD+, NADPH, and NADP+were measured in cells expressing transhydrogenase. The reduction of the NADPH pool indicated that the transhydrogenase transferred reducing equivalents from NADPH to NAD+.
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2

Tsai, C. Stan, and D. J. Senior. "Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria." Biochemistry and Cell Biology 68, no. 4 (April 1, 1990): 751–57. http://dx.doi.org/10.1139/o90-108.

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Various kinetic approaches were carried out to investigate kinetic attributes for the dual coenzyme activities of mitochondrial aldehyde dehydrogenase from rat liver. The enzyme catalyses NAD+- and NADP+-dependent oxidations of ethanal by an ordered bi-bi mechanism with NAD(P)+ as the first reactant bound and NAD(P)H as the last product released. The two coenzymes presumably interact with the kinetically identical site. NAD+ forms the dynamic binary complex with the enzyme, while the enzyme-NAD(P)H complex formation is associated with conformation change(s). A stopped-flow burst of NAD(P)H formation, followed by a slower steady-state turnover, suggests that either the deacylation or the release of NAD(P)H is rate limiting. Although NADP+ is reduced by a faster burst rate, NAD+ is slightly favored as the coenzyme by virtue of its marginally faster turnover rate.Key words: aldehyde dehydrogenase, coenzyme preference.
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3

Liu, Si-Qi, Hongjun Jin, Albert Zacarias, Sanjay Srivastava, and Aruni Bhatnagar. "Binding of Pyridine Nucleotide Coenzymes to the β-Subunit of the Voltage-sensitive K+Channel." Journal of Biological Chemistry 276, no. 15 (January 17, 2001): 11812–20. http://dx.doi.org/10.1074/jbc.m008259200.

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The β-subunit of the voltage-sensitive K+(Kv) channels belongs to the aldo-keto reductase superfamily, and the crystal structure of Kvβ2 shows NADP bound in its active site. Here we report that Kvβ2 displays a high affinity for NADPH (Kd= 0.1 μm) and NADP+(Kd= 0.3 μm), as determined by fluorometric titrations of the recombinant protein. The Kvβ2 also bound NAD(H) but with 10-fold lower affinity. The site-directed mutants R264E and N333W did not bind NADPH, whereas, theKdNADPHof Q214R was 10-fold greater than the wild-type protein. TheKdNADPHwas unaffected by the R189M, W243Y, W243A, or Y255F mutation. The tetrameric structure of the wild-type protein was retained by the R264E mutant, indicating that NADPH binding is not a prerequisite for multimer formation. A C248S mutation caused a 5-fold decrease inKdNADPH, shifted the pKaofKdNADPHfrom 6.9 to 7.4, and decreased the ionic strength dependence of NADPH binding. These results indicate that Arg-264 and Asn-333 are critical for coenzyme binding, which is regulated in part by Cys-248. The binding of both NADP(H) and NAD(H) to the protein suggests that several types of Kvβ2-nucleotide complexes may be formedin vivo.
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4

Pfoh, Roland, Emil F. Pai, and Vivian Saridakis. "Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides." Acta Crystallographica Section D Biological Crystallography 71, no. 10 (September 26, 2015): 2032–39. http://dx.doi.org/10.1107/s1399004715015497.

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Nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes the biosynthesis of NAD+and NaAD+. The crystal structure of NMNAT fromMethanobacterium thermoautotrophicumcomplexed with NAD+and SO42−revealed the active-site residues involved in binding and catalysis. Site-directed mutagenesis was used to further characterize the roles played by several of these residues. Arg11 and Arg136 were implicated in binding the phosphate groups of the ATP substrate. Both of these residues were mutated to lysine individually. Arg47 does not interact with either NMN or ATP substrates directly, but was deemed to play a role in binding as it is proximal to Arg11 and Arg136. Arg47 was mutated to lysine and glutamic acid. Surprisingly, when expressed inEscherichia coliall of these NMNAT mutants trapped a molecule of NADP+in their active sites. This NADP+was bound in a conformation that was quite different from that displayed by NAD+in the native enzyme complex. When NADP+was co-crystallized with wild-type NMNAT, the same structural arrangement was observed. These studies revealed a different conformation of NADP+in the active site of NMNAT, indicating plasticity of the active site.
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5

Okai, Masahiko, Norio Kudo, Woo Cheol Lee, Masayuki Kamo, Koji Nagata, and Masaru Tanokura. "Crystal Structures of the Short-Chain Flavin Reductase HpaC fromSulfolobus tokodaiiStrain 7 in Its Three States: NAD(P)+-Free, NAD+-Bound, and NADP+-Bound†,‡." Biochemistry 45, no. 16 (April 2006): 5103–10. http://dx.doi.org/10.1021/bi052313i.

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6

Takei, H., K. Nakashima, O. Adachi, E. Shinagawa, and M. Ameyama. "Enzymatic determination of serum ethanol with membrane-bound dehydrogenase." Clinical Chemistry 31, no. 12 (December 1, 1985): 1985–87. http://dx.doi.org/10.1093/clinchem/31.12.1985.

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Abstract In this enzymatic method for detecting ethanol in blood by use of membrane-bound microbial alcohol dehydrogenase (no EC no. assigned), the enzyme catalyzes the reaction irreversibly and the rate of oxidation can be monitored by spectrophotometry of the reduction of the indicator dye. No pyridine nucleotides such as NAD+ or NADP+ are used. The calibration curve is linear in the range of 0.1 to 4.0 g of ethanol per liter. Assays of 45 samples of serum having ethanol values ranging from 0.4 to 3.2 g/L by the described technique and a gas-chromatographic method gave respective means of 1.734 and 1.732 g/L (r = 0.954).
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7

MATSUURA, Kazuya, Yoshiyuki TAMADA, Kumiko SATO, Harunori IWASA, Gunpei MIWA, Yoshihiro DEYASHIKI, and Akira HARA. "Involvement of two basic residues (Lys-270 and Arg-276) of human liver 3α-hydroxysteroid dehydrogenase in NADP(H) binding and activation by sulphobromophthalein: site-directed mutagenesis and kinetic analysis." Biochemical Journal 322, no. 1 (February 15, 1997): 89–93. http://dx.doi.org/10.1042/bj3220089.

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A human liver 3α-hydroxysteroid dehydrogenase isoenzyme, a member of the aldoŐketo reductase family, shows a marked preference for NADP(H) over NAD(H), and is activated by sulphobromophthalein, which increases the Km values for both NADP(H) and substrates. Here we report kinetic alterations in binding of the coenzymes and the activator to the enzyme caused by site-directed mutagenesis of Lys-270 and Arg-276, which are strictly conserved among the aldoŐketo reductase family of enzymes. The mutated enzymes, K270M and R276M, showed increases in the Km for NADP+ of 22- and 290-fold respectively; the Km for alcohol substrate and the kcat of the NADP+-linked reaction were also elevated, by 9- and 5-fold respectively. No kinetic constant of the NAD+-linked reaction was altered by more than 3-fold. Calculation of the free-energy changes showed that the 2ƀ-phosphate group of NADP+ contributes 16.3 kJ/mol (3.9 kcal/mol) of binding energy to its interaction with the wild-type enzyme, and the mutagenesis to K270M and R276M destabilized the binding energy of NADP+ by 6.3 and 13.0 kJ/mol (1.5 and 3.1 kcal/mol) respectively. In addition, the mutations attenuated enzyme activation by sulphobromophthalein, which bound to the mutant enzymes as an inhibitor. The inhibition for the R276M mutant was competitive with respect to NADP+ and non-competitive with respect to the substrate, whereas that for the K270M mutant was mixed-type, showing activation at coenzyme concentrations greater than 20ȕKm. These results suggest that the two basic residues in the 3α-hydroxysteroid dehydrogenase isoenzyme play crucial roles in binding both the negatively charged 2ƀ-phosphate group of NADP+ and the sulphonic groups of sulphobromophthalein.
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8

Sugishima, Masakazu, Kei Wada, and Keiichi Fukuyama. "Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures." Current Medicinal Chemistry 27, no. 21 (June 15, 2020): 3499–518. http://dx.doi.org/10.2174/0929867326666181217142715.

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In mammals, catabolism of the heme group is indispensable for life. Heme is first cleaved by the enzyme Heme Oxygenase (HO) to the linear tetrapyrrole Biliverdin IXα (BV), and BV is then converted into bilirubin by Biliverdin Reductase (BVR). HO utilizes three Oxygen molecules (O2) and seven electrons supplied by NADPH-cytochrome P450 oxidoreductase (CPR) to open the heme ring and BVR reduces BV through the use of NAD(P)H. Structural studies of HOs, including substrate-bound, reaction intermediate-bound, and several specific inhibitor-bound forms, reveal details explaining substrate binding to HO and mechanisms underlying-specific HO reaction progression. Cryo-trapped structures and a time-resolved spectroscopic study examining photolysis of the bond between the distal ligand and heme iron demonstrate how CO, produced during the HO reaction, dissociates from the reaction site with a corresponding conformational change in HO. The complex structure containing HO and CPR provides details of how electrons are transferred to the heme-HO complex. Although the tertiary structure of BVR and its complex with NAD+ was determined more than 10 years ago, the catalytic residues and the reaction mechanism of BVR remain unknown. A recent crystallographic study examining cyanobacterial BVR in complex with NADP+ and substrate BV provided some clarification regarding these issues. Two BV molecules are bound to BVR in a stacked manner, and one BV may assist in the reductive catalysis of the other BV. In this review, recent advances illustrated by biochemical, spectroscopic, and crystallographic studies detailing the chemistry underlying the molecular mechanism of HO and BVR reactions are presented.
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9

KAVANAGH, Kathryn L., Mario KLIMACEK, Bernd NIDETZKY, and David K. WILSON. "Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases." Biochemical Journal 373, no. 2 (July 15, 2003): 319–26. http://dx.doi.org/10.1042/bj20030286.

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Xylose reductase (XR; AKR2B5) is an unusual member of aldo-keto reductase superfamily, because it is one of the few able to efficiently utilize both NADPH and NADH as co-substrates in converting xylose into xylitol. In order to better understand the basis for this dual specificity, we have determined the crystal structure of XR from the yeast Candida tenuis in complex with NAD+ to 1.80 Å resolution (where 1 Å=0.1 nm) with a crystallographic R-factor of 18.3%. A comparison of the NAD+- and the previously determined NADP+-bound forms of XR reveals that XR has the ability to change the conformation of two loops. To accommodate both the presence and absence of the 2′-phosphate, the enzyme is able to adopt different conformations for several different side chains on these loops, including Asn276, which makes alternative hydrogen-bonding interactions with the adenosine ribose. Also critical is the presence of Glu227 on a short rigid helix, which makes hydrogen bonds to both the 2′- and 3′-hydroxy groups of the adenosine ribose. In addition to changes in hydrogen-bonding of the adenosine, the ribose unmistakably adopts a 3′-endo conformation rather than the 2′-endo conformation seen in the NADP+-bound form. These results underscore the importance of tight adenosine binding for efficient use of either NADH or NADPH as a co-substrate in aldo-keto reductases. The dual specificity found in XR is also an important consideration in designing a high-flux xylose metabolic pathway, which may be improved with an enzyme specific for NADH.
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10

Argyrou, Argyrides, Matthew W. Vetting, and John S. Blanchard. "Characterization of a New Member of the Flavoprotein Disulfide Reductase Family of Enzymes fromMycobacterium tuberculosis." Journal of Biological Chemistry 279, no. 50 (September 29, 2004): 52694–702. http://dx.doi.org/10.1074/jbc.m410704200.

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ThelpdA(Rv3303c) gene fromMycobacterium tuberculosisencoding a new member of the flavoprotein disulfide reductases was expressed inEscherichia coli, and the recombinant LpdA protein was purified to homogeneity. LpdA is a homotetramer and co-purifies with one molecule of tightly but noncovalently bound FAD and NADP+per monomer. Although annotated as a probable lipoamide dehydrogenase inM. tuberculosis, LpdA cannot catalyze reduction of lipoyl substrates, because it lacks one of two cysteine residues involved in dithiol-disulfide interchange with lipoyl substrates and a His-Glu pair involved in general acid catalysis. The crystal structure of LpdA was solved by multiple isomorphous replacement with anomalous scattering, which confirmed the absence of these catalytic residues from the active site. Although LpdA cannot catalyze reduction of disulfide-bonded substrates, it catalyzes the NAD(P)H-dependent reduction of alternative electron acceptors such as 2,6-dimethyl-1,4-benzoquinone and 5-hydroxy-1,4-naphthaquinone. Significant primary deuterium kinetic isotope effects were observed with [4S-2H]NADH establishing that the enzyme promotes transfer of the C4-proShydride of NADH. The absence of an isotope effect with [4S-2H]NADPH, the lowKmvalue of 0.5 μmfor NADPH, and the potent inhibition of the NADH-dependent reduction of 2,6-dimethyl-1,4-benzoquinone by NADP+(Ki∼ 6 nm) and 2′-phospho-ADP-ribose (Ki∼ 800 nm), demonstrate the high affinity of LpdA for 2′-phosphorylated nucleotides and that the physiological substrate/product pair is NADPH/NADP+rather than NADH/NAD+. Modeling of NADP+in the active site revealed that LpdA achieves the high specificity for NADP+through interactions involving the 2′-phosphate of NADP+and amino acid residues that are different from those in glutathione reductase.
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Dissertations / Theses on the topic "NADP-bound; NAD-bound"

1

Naylor, Claire. "X-ray crystallographic studies of glucose 6-phosphate dehydrogenase." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.360467.

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