메뉴 건너뛰기




Volumn 178, Issue 1-3, 2009, Pages 165-170

Kinetics of nucleotide binding to the β-subunit (AKR6A2) of the voltage-gated potassium (Kv) channel

Author keywords

Aldo keto reductases; Kinetics; Kv channel; Kv subunits; Nucleotide binding

Indexed keywords

ALDEHYDE REDUCTASE; ALDO KETO REDUCTASE 6A2; BENZALDEHYDE DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 59049087574     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.10.016     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0028609781 scopus 로고
    • + channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily
    • + channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell 79 (1994) 1133-1135
    • (1994) Cell , vol.79 , pp. 1133-1135
    • McCormack, T.1    McCormack, K.2
  • 3
    • 0032567505 scopus 로고    scopus 로고
    • Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium
    • Leicher T., Bahring R., Isbrandt D., and Pongs O. Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium. J. Biol. Chem. 273 (1998) 35095-35101
    • (1998) J. Biol. Chem. , vol.273 , pp. 35095-35101
    • Leicher, T.1    Bahring, R.2    Isbrandt, D.3    Pongs, O.4
  • 10
    • 59049083667 scopus 로고    scopus 로고
    • Catalytic activity of the beta-subunits of the voltage-gated potassium channels and its regulation by pyridine nucleotides
    • Weiner H., Maser E., Lindahl R., and Plapp B. (Eds), Purdue University Press, West Lafayette, Indiana
    • Tipparaju S.M., Bhatnagar A., and Barski O.A. Catalytic activity of the beta-subunits of the voltage-gated potassium channels and its regulation by pyridine nucleotides. In: Weiner H., Maser E., Lindahl R., and Plapp B. (Eds). Enzymology and Molecular Biology of Carbonyl Metabolism (2006), Purdue University Press, West Lafayette, Indiana 401-410
    • (2006) Enzymology and Molecular Biology of Carbonyl Metabolism , pp. 401-410
    • Tipparaju, S.M.1    Bhatnagar, A.2    Barski, O.A.3
  • 11
    • 33744970273 scopus 로고    scopus 로고
    • Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase
    • Weng J., Cao Y., Moss N., and Zhou M. Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase. J. Biol. Chem. 281 (2006) 15194-15200
    • (2006) J. Biol. Chem. , vol.281 , pp. 15194-15200
    • Weng, J.1    Cao, Y.2    Moss, N.3    Zhou, M.4
  • 12
    • 50149118166 scopus 로고    scopus 로고
    • Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel
    • Tipparaju S.M., Barski O.A., Srivastava S., and Bhatnagar A. Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel. Biochemistry 47 (2008) 8840-8854
    • (2008) Biochemistry , vol.47 , pp. 8840-8854
    • Tipparaju, S.M.1    Barski, O.A.2    Srivastava, S.3    Bhatnagar, A.4
  • 13
    • 43749106478 scopus 로고    scopus 로고
    • Functional coupling between the Kv1.1 channel and aldoketoreductase Kvbeta1
    • Pan Y., Weng J., Cao Y., Bhosle R.C., and Zhou M. Functional coupling between the Kv1.1 channel and aldoketoreductase Kvbeta1. J. Biol. Chem. 283 (2008) 8634-8642
    • (2008) J. Biol. Chem. , vol.283 , pp. 8634-8642
    • Pan, Y.1    Weng, J.2    Cao, Y.3    Bhosle, R.C.4    Zhou, M.5
  • 14
    • 0028837692 scopus 로고
    • Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme
    • Grimshaw C.E., Bohren K.M., Lai C.J., and Gabbay K.H. Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme. Biochemistry 34 (1995) 14356-14365
    • (1995) Biochemistry , vol.34 , pp. 14356-14365
    • Grimshaw, C.E.1    Bohren, K.M.2    Lai, C.J.3    Gabbay, K.H.4
  • 15
    • 0026701774 scopus 로고
    • Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding
    • Kubiseski T.J., Hyndman D.J., Morjana N.A., and Flynn T.G. Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding. J Biol. Chem. 267 (1992) 6510-6517
    • (1992) J Biol. Chem. , vol.267 , pp. 6510-6517
    • Kubiseski, T.J.1    Hyndman, D.J.2    Morjana, N.A.3    Flynn, T.G.4
  • 16
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson D.K., Bohren K.M., Gabbay K.H., and Quiocho F.A. An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257 (1992) 81-84
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0035969828 scopus 로고    scopus 로고
    • Binding of pyridine coenzymes to the beta-subunit of the voltage sensitive potassium channels
    • Liu S.Q., Jin H., Zacarias A., Srivastava S., and Bhatnagar A. Binding of pyridine coenzymes to the beta-subunit of the voltage sensitive potassium channels. Chem. Biol. Interact. 130-132 (2001) 955-962
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 955-962
    • Liu, S.Q.1    Jin, H.2    Zacarias, A.3    Srivastava, S.4    Bhatnagar, A.5
  • 19
    • 0015608091 scopus 로고
    • Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases
    • Stinson R.A., and Holbrook J.J. Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases. Biochem. J. 131 (1973) 719-728
    • (1973) Biochem. J. , vol.131 , pp. 719-728
    • Stinson, R.A.1    Holbrook, J.J.2
  • 20
    • 0029103124 scopus 로고
    • Mechanism of human aldehyde reductase: characterization of the active site pocket
    • Barski O.A., Gabbay K.H., Grimshaw C.E., and Bohren K.M. Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34 (1995) 11264-11275
    • (1995) Biochemistry , vol.34 , pp. 11264-11275
    • Barski, O.A.1    Gabbay, K.H.2    Grimshaw, C.E.3    Bohren, K.M.4
  • 21
    • 33751096178 scopus 로고    scopus 로고
    • Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens
    • Jin Y., and Penning T.M. Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens. Biochemistry 45 (2006) 13054-13063
    • (2006) Biochemistry , vol.45 , pp. 13054-13063
    • Jin, Y.1    Penning, T.M.2
  • 22
    • 0035964171 scopus 로고    scopus 로고
    • Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis
    • Nidetzky B., Klimacek M., and Mayr P. Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tenuis. Biochemistry 40 (2001) 10371-10381
    • (2001) Biochemistry , vol.40 , pp. 10371-10381
    • Nidetzky, B.1    Klimacek, M.2    Mayr, P.3
  • 24
    • 0028229517 scopus 로고
    • Overexpression and mutagenesis of the cDNA for rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis
    • Pawlowski J.E., and Penning T.M. Overexpression and mutagenesis of the cDNA for rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis. J. Biol. Chem. 269 (1994) 13502-13510
    • (1994) J. Biol. Chem. , vol.269 , pp. 13502-13510
    • Pawlowski, J.E.1    Penning, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.