ABCC7 p.Lys464Leu
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PMID: 9511928
[PubMed]
Seibert FS et al: "Cystic fibrosis: channel, catalytic, and folding properties of the CFTR protein."
No.
Sentence
Comment
101
The observed Vmax of ~30 nmol/mg/min is very low compared to other ATPases such as the Ca++ -ATPase (600 nmol/mg/min; Racker, 1985) or P-glycoprotein (300-1650 nmol/mg/min; Sharom et al., 1995), although an indication of the significance of the data is given by a negative effect due to Walker A mutations K464H and K464L.
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ABCC7 p.Lys464Leu 9511928:101:316
status: NEW
PMID: 7545672
[PubMed]
Ko YH et al: "The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase."
No.
Sentence
Comment
4
Significantly, the mutations K464H and K464L in the Walker A consensus motif of NBF1 markedly impair its catalytic capacity.
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ABCC7 p.Lys464Leu 7545672:4:39
status: NEW43 K464H: 5Ј-ACT GGA GCA GGC CAC ACT TCA CTT CTA-3Ј K464L: 5Ј-ACT GGA GCA GGC CTG ACT TCA CTT CTA-3Ј The identity of the two base changes was confirmed by DNA sequencing (20).
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ABCC7 p.Lys464Leu 7545672:43:61
status: NEW113 B, comparison of the purity of wild type and mutant MBP-NBF1 proteins (K464H and K464L).
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ABCC7 p.Lys464Leu 7545672:113:81
status: NEW115 C and D, the effect of the mutations K464H and K464L within NBF1 on the ATP hydrolytic activity of MBP-NBF1.
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ABCC7 p.Lys464Leu 7545672:115:47
status: NEW125 Even more convincing are results presented in Fig. 4, C and D, where it is seen that the mutations, K464H and K464L, in the Walker A nucleotide binding motif (GX4GKT) of NBF1 reduce the ATP hydrolytic capacity of purified mutant MBP-NBF1 proteins by over 80%.
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ABCC7 p.Lys464Leu 7545672:125:110
status: NEW133 The additional experimental results demonstrating that MBP alone has no catalytic capacity (Fig. 2C) and that mutations (K464H and K464L) within the Walker nucleotide binding motif GX4GKT markedly inhibit ATPase activity (Fig. 4, C and D) localize the catalytic site to NBF1.
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ABCC7 p.Lys464Leu 7545672:133:131
status: NEW42 K464H: 59-ACT GGA GCA GGC CAC ACT TCA CTT CTA-39 K464L: 59-ACT GGA GCA GGC CTG ACT TCA CTT CTA-39 The identity of the two base changes was confirmed by DNA sequencing (20).
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ABCC7 p.Lys464Leu 7545672:42:49
status: NEW112 B, comparison of the purity of wild type and mutant MBP-NBF1 proteins (K464H and K464L).
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ABCC7 p.Lys464Leu 7545672:112:81
status: NEW114 C and D, the effect of the mutations K464H and K464L within NBF1 on the ATP hydrolytic activity of MBP-NBF1.
X
ABCC7 p.Lys464Leu 7545672:114:47
status: NEW124 Even more convincing are results presented in Fig. 4, C and D, where it is seen that the mutations, K464H and K464L, in the Walker A nucleotide binding motif (GX4GKT) of NBF1 reduce the ATP hydrolytic capacity of purified mutant MBP-NBF1 proteins by over 80%.
X
ABCC7 p.Lys464Leu 7545672:124:110
status: NEW132 The additional experimental results demonstrating that MBP alone has no catalytic capacity (Fig. 2C) and that mutations (K464H and K464L) within the Walker nucleotide binding motif GX4GKT markedly inhibit ATPase activity (Fig. 4, C and D) localize the catalytic site to NBF1.
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ABCC7 p.Lys464Leu 7545672:132:131
status: NEW