ABCD3 p.Ser572Ile

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PMID: 12530690 [PubMed] Gartner J et al: "Functional characterization of the adrenoleukodystrophy protein (ALDP) and disease pathogenesis."
No. Sentence Comment
41 The mutant constructs included missense mutations of patients with X-ALD in the nucleotide binding fold regions Walker A and 19mer (ALDP-NBF-G512S, ALDP-NBF-Q544R, ALDP-NBF-P560L, ALDP-NBF-R591Q, ALDP-NBF-S606L, and ALDP-NBF-D629H) and corresponding mutations in another ABC transporter in the peroxisome membrane, the 70 kDa peroxisomal membrane protein (PMP70; PMP70-NBF-G478R, PMP70- NBF-S572I).
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ABCD3 p.Ser572Ile 12530690:41:391
status: NEW
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63 The mutation S572I in the PMP70 gene reduces considerable ATPase activity where as the mutation G478R alters ATP-binding affinity.
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ABCD3 p.Ser572Ile 12530690:63:13
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PMID: 11248239 [PubMed] Roerig P et al: "Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters."
No. Sentence Comment
5 Mutations in conserved residues of the nucleotidases (PMP70: G478R, S572I; ALDP: G512S, S606L) altered ATPase activity.
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ABCD3 p.Ser572Ile 11248239:5:68
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24 For the mutant constructs we selected X-ALD patient mutations in highly conserved residues in the Walker A and 19-mer region of the NBF of ALDP (G512S and S606L) and the corresponding PMP70 mutations (G478R and S572I).
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ABCD3 p.Ser572Ile 11248239:24:211
status: NEW
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85 Additionally, we changed the conserved serine in the 19-mer motif of PMP70 and ALDP to isoleucine (S572I) and leucine (S606L), respectively.
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ABCD3 p.Ser572Ile 11248239:85:99
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88 The K-subunit of L-galactosidase (L-Protein Synthetic oligonucleotide Mutation ALDP 5P-CCCCAATGGCTGCAGCAAGAGCTCCC-3P G512S 5P-GGATCCGGACAGGGAGCTCTTGCTGCAGC-3P ALDP 5P-ACTGGAAGGACGTCCTGTTGGG-3P S606L 5P-CGCCACCCAACAGGACGTCCTTCC-3P PMP70 5P-GGCTGCAGAAAGAGTTCACTTTTCCG-3P G478R 5P-GGCCATAATTCACCAAGAACACGGAAA AGTGAACTCTTTCTG-3P PMP70 5P-GACGTACTCATTGGTGGAG-3P S572I 5P-CCACCAATGAGTACGTCCATCCAATCC-3P gal) in fusion with the MBP was used as a control.
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ABCD3 p.Ser572Ile 11248239:88:357
status: NEW
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136 The S606L and G478R mutants have a decreased ATP binding a¤nity while the G512S and S572I mutants decrease the maximum velocity of ATPase activity.
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ABCD3 p.Ser572Ile 11248239:136:89
status: NEW
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182 Previous studies on MDR suggest that the ATPase activity of the native protein Table 1 Kinetic parameters of ATPase activity in wild type and mutant ALDP and PMP70 NBF fusion proteins Fusion protein KM (WM) Vmax (nmol/Wmol NBF/min) Speci'c activity (1033 U/mg) ALDP (wild type) 11.5 þ 0.97 641.9 þ 10.7 10.0 þ 0.17 ALDP (G512S) 17.9 þ 1.23 279.3 þ 4.2 4.4 þ 0.06 ALDP (S606L) 45.6 þ 2.40 666.0 þ 8.7 10.4 þ 0.14 PMP70 (wild type) 8.2 þ 0.52 580.8 þ 6.7 9.0 þ 0.10 PMP70 (G478R) 161.8 þ 34.40 641.2 þ 28.2 10.0 þ 0.44 PMP70 (S572I) 9.9 þ 0.82 298.1 þ 4.7 4.6 þ 0.07 The kinetic data of all fusion proteins are mean values and standard deviations of 15^20 measurements at various protein concentrations using at least two distinct protein preparations.
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ABCD3 p.Ser572Ile 11248239:182:599
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86 Additionally, we changed the conserved serine in the 19-mer motif of PMP70 and ALDP to isoleucine (S572I) and leucine (S606L), respectively.
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ABCD3 p.Ser572Ile 11248239:86:99
status: NEW
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89 The K-subunit of L-galactosidase (LProtein Synthetic oligonucleotide Mutation ALDP 5P-CCCCAATGGCTGCAGCAAGAGCTCCC-3P G512S 5P-GGATCCGGACAGGGAGCTCTTGCTGCAGC-3P ALDP 5P-ACTGGAAGGACGTCCTGTTGGG-3P S606L 5P-CGCCACCCAACAGGACGTCCTTCC-3P PMP70 5P-GGCTGCAGAAAGAGTTCACTTTTCCG-3P G478R 5P-GGCCATAATTCACCAAGAACACGGAAA AGTGAACTCTTTCTG-3P PMP70 5P-GACGTACTCATTGGTGGAG-3P S572I 5P-CCACCAATGAGTACGTCCATCCAATCC-3P gal) in fusion with the MBP was used as a control.
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ABCD3 p.Ser572Ile 11248239:89:356
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137 The S606L and G478R mutants have a decreased ATP binding a&#a4;nity while the G512S and S572I mutants decrease the maximum velocity of ATPase activity.
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ABCD3 p.Ser572Ile 11248239:137:88
status: NEW
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183 Previous studies on MDR suggest that the ATPase activity of the native protein Table 1 Kinetic parameters of ATPase activity in wild type and mutant ALDP and PMP70 NBF fusion proteins Fusion protein KM (WM) Vmax (nmol/Wmol NBF/min) Speci'c activity (1033 U/mg) ALDP (wild type) 11.5 &#fe; 0.97 641.9 &#fe; 10.7 10.0 &#fe; 0.17 ALDP (G512S) 17.9 &#fe; 1.23 279.3 &#fe; 4.2 4.4 &#fe; 0.06 ALDP (S606L) 45.6 &#fe; 2.40 666.0 &#fe; 8.7 10.4 &#fe; 0.14 PMP70 (wild type) 8.2 &#fe; 0.52 580.8 &#fe; 6.7 9.0 &#fe; 0.10 PMP70 (G478R) 161.8 &#fe; 34.40 641.2 &#fe; 28.2 10.0 &#fe; 0.44 PMP70 (S572I) 9.9 &#fe; 0.82 298.1 &#fe; 4.7 4.6 &#fe; 0.07 The kinetic data of all fusion proteins are mean values and standard deviations of 15^20 measurements at various protein concentrations using at least two distinct protein preparations.
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ABCD3 p.Ser572Ile 11248239:183:584
status: NEW
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