1auk: Difference between revisions

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<StructureSection load='1auk' size='340' side='right'caption='[[1auk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1auk' size='340' side='right'caption='[[1auk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1auk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1AUK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1auk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FGL:2-AMINOPROPANEDIOIC+ACID'>FGL</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FGL:2-AMINOPROPANEDIOIC+ACID'>FGL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1auk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auk OCA], [https://pdbe.org/1auk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auk RCSB], [https://www.ebi.ac.uk/pdbsum/1auk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auk ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cerebroside-sulfatase Cerebroside-sulfatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.8 3.1.6.8] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1auk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auk OCA], [http://pdbe.org/1auk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auk RCSB], [http://www.ebi.ac.uk/pdbsum/1auk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1auk ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/ARSA_HUMAN ARSA_HUMAN]] Defects in ARSA are a cause of leukodystrophy metachromatic (MLD) [MIM:[http://omim.org/entry/250100 250100]]. MLD is a disease due to a lysosomal storage defect. It is characterized by intralysosomal storage of cerebroside-3-sulfate in neural and non-neural tissues, with a diffuse loss of myelin in the central nervous system. Progressive demyelination causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Three forms of the disease can be distinguished according to the age at onset: late-infantile, juvenile and adult.<ref>PMID:1673291</ref> <ref>PMID:1678251</ref> <ref>PMID:1670590</ref> <ref>PMID:1353340</ref> <ref>PMID:8101038</ref> <ref>PMID:8101083</ref> <ref>PMID:8095918</ref> <ref>PMID:7902317</ref> <ref>PMID:7906588</ref> <ref>PMID:8104633</ref> <ref>PMID:7909527</ref> <ref>PMID:7825603</ref> <ref>PMID:7860068</ref> <ref>PMID:7581401</ref> <ref>PMID:8891236</ref> <ref>PMID:9272717</ref> <ref>PMID:9090526</ref> <ref>PMID:9490297</ref> <ref>PMID:9600244</ref> <ref>PMID:9452102</ref> <ref>PMID:9819708</ref> <ref>PMID:10220151</ref> <ref>PMID:10477432</ref> <ref>PMID:10533072</ref> <ref>PMID:10381328</ref> <ref>PMID:10751093</ref> <ref>PMID:11061266</ref> <ref>PMID:11020646</ref> <ref>PMID:11456299</ref> <ref>PMID:11941485</ref> <ref>PMID:12503099</ref> <ref>PMID:12788103</ref> <ref>PMID:14517960</ref> <ref>PMID:14680985</ref> <ref>PMID:15326627</ref> <ref>PMID:15026521</ref> <ref>PMID:15710861</ref> <ref>PMID:18693274</ref> <ref>PMID:19606494</ref> <ref>PMID:20339381</ref> <ref>PMID:21265945</ref>  Arylsulfatase A activity is defective in multiple sulfatase deficiency (MSD) [MIM:[http://omim.org/entry/272200 272200]]. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Note=Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3-oxoalanine.<ref>PMID:7628016</ref> <ref>PMID:15146462</ref>
[https://www.uniprot.org/uniprot/ARSA_HUMAN ARSA_HUMAN] Defects in ARSA are a cause of leukodystrophy metachromatic (MLD) [MIM:[https://omim.org/entry/250100 250100]. MLD is a disease due to a lysosomal storage defect. It is characterized by intralysosomal storage of cerebroside-3-sulfate in neural and non-neural tissues, with a diffuse loss of myelin in the central nervous system. Progressive demyelination causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Three forms of the disease can be distinguished according to the age at onset: late-infantile, juvenile and adult.<ref>PMID:1673291</ref> <ref>PMID:1678251</ref> <ref>PMID:1670590</ref> <ref>PMID:1353340</ref> <ref>PMID:8101038</ref> <ref>PMID:8101083</ref> <ref>PMID:8095918</ref> <ref>PMID:7902317</ref> <ref>PMID:7906588</ref> <ref>PMID:8104633</ref> <ref>PMID:7909527</ref> <ref>PMID:7825603</ref> <ref>PMID:7860068</ref> <ref>PMID:7581401</ref> <ref>PMID:8891236</ref> <ref>PMID:9272717</ref> <ref>PMID:9090526</ref> <ref>PMID:9490297</ref> <ref>PMID:9600244</ref> <ref>PMID:9452102</ref> <ref>PMID:9819708</ref> <ref>PMID:10220151</ref> <ref>PMID:10477432</ref> <ref>PMID:10533072</ref> <ref>PMID:10381328</ref> <ref>PMID:10751093</ref> <ref>PMID:11061266</ref> <ref>PMID:11020646</ref> <ref>PMID:11456299</ref> <ref>PMID:11941485</ref> <ref>PMID:12503099</ref> <ref>PMID:12788103</ref> <ref>PMID:14517960</ref> <ref>PMID:14680985</ref> <ref>PMID:15326627</ref> <ref>PMID:15026521</ref> <ref>PMID:15710861</ref> <ref>PMID:18693274</ref> <ref>PMID:19606494</ref> <ref>PMID:20339381</ref> <ref>PMID:21265945</ref>  Arylsulfatase A activity is defective in multiple sulfatase deficiency (MSD) [MIM:[https://omim.org/entry/272200 272200]. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Note=Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3-oxoalanine.<ref>PMID:7628016</ref> <ref>PMID:15146462</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ARSA_HUMAN ARSA_HUMAN]] Hydrolyzes cerebroside sulfate.  
[https://www.uniprot.org/uniprot/ARSA_HUMAN ARSA_HUMAN] Hydrolyzes cerebroside sulfate.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1auk ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1auk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human lysosomal arylsulfatase A (ASA) is a prototype member of the sulfatase family. These enzymes require the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine. Without this modification sulfatases are catalytically inactive, as revealed by a lysosomal storage disorder known as multiple sulfatase deficiency. The 2.1 A resolution X-ray crystal structure shows an ASA homooctamer composed of a tetramer of dimers, (alpha 2)4. The alpha/beta fold of the monomer has significant structural analogy to another hydrolytic enzyme, the alkaline phosphatase, and superposition of these two structures shows that the active centers are located in largely identical positions. The functionally essential formylglycine is located in a positively charged pocket and acts as ligand to an octahedrally coordinated metal ion interpreted as Mg2+. The electron density at the formylglycine suggests the presence of a 2-fold disordered aldehyde group with the possible contribution of an aldehyde hydrate, -CH(OH)2, with gem-hydroxyl groups. In the proposed catalytic mechanism, the aldehyde accepts a water molecule to form a hydrate. One of the two hydroxyl groups hydrolyzes the substrate sulfate ester via a transesterification step, resulting in a covalent intermediate. The second hydroxyl serves to eliminate sulfate under inversion of configuration through C-O cleavage and reformation of the aldehyde. This study provides the structural basis for understanding a novel mechanism of ester hydrolysis and explains the functional importance of the unusually modified amino acid.
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.,Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W Biochemistry. 1998 Mar 17;37(11):3654-64. PMID:9521684<ref>PMID:9521684</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1auk" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cerebroside-sulfatase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Figura, K Von]]
[[Category: Gieselmann V]]
[[Category: Gieselmann, V]]
[[Category: Krauss N]]
[[Category: Krauss, N]]
[[Category: Lukatela G]]
[[Category: Lukatela, G]]
[[Category: Saenger W]]
[[Category: Saenger, W]]
[[Category: Theis K]]
[[Category: Theis, K]]
[[Category: Von Figura K]]
[[Category: Cerebroside-3-sulfate hydrolysis]]
[[Category: Hydrolase]]
[[Category: Lysosomal enzyme]]

Latest revision as of 18:28, 13 March 2024

HUMAN ARYLSULFATASE AHUMAN ARYLSULFATASE A

Structural highlights

1auk is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ARSA_HUMAN Defects in ARSA are a cause of leukodystrophy metachromatic (MLD) [MIM:250100. MLD is a disease due to a lysosomal storage defect. It is characterized by intralysosomal storage of cerebroside-3-sulfate in neural and non-neural tissues, with a diffuse loss of myelin in the central nervous system. Progressive demyelination causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Three forms of the disease can be distinguished according to the age at onset: late-infantile, juvenile and adult.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40] [41] Arylsulfatase A activity is defective in multiple sulfatase deficiency (MSD) [MIM:272200. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Note=Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3-oxoalanine.[42] [43]

Function

ARSA_HUMAN Hydrolyzes cerebroside sulfate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Kondo R, Wakamatsu N, Yoshino H, Fukuhara N, Miyatake T, Tsuji S. Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. Am J Hum Genet. 1991 May;48(5):971-8. PMID:1673291
  2. ↑ Gieselmann V, Fluharty AL, Tonnesen T, Von Figura K. Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. Am J Hum Genet. 1991 Aug;49(2):407-13. PMID:1678251
  3. ↑ Polten A, Fluharty AL, Fluharty CB, Kappler J, von Figura K, Gieselmann V. Molecular basis of different forms of metachromatic leukodystrophy. N Engl J Med. 1991 Jan 3;324(1):18-22. PMID:1670590
  4. ↑ Kappler J, von Figura K, Gieselmann V. Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. Ann Neurol. 1992 Mar;31(3):256-61. PMID:1353340 doi:http://dx.doi.org/10.1002/ana.410310305
  5. ↑ Kreysing J, Bohne W, Bosenberg C, Marchesini S, Turpin JC, Baumann N, von Figura K, Gieselmann V. High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. Am J Hum Genet. 1993 Aug;53(2):339-46. PMID:8101038
  6. ↑ Hasegawa Y, Kawame H, Eto Y. Mutations in the arylsulfatase A gene of Japanese patients with metachromatic leukodystrophy. DNA Cell Biol. 1993 Jul-Aug;12(6):493-8. PMID:8101083
  7. ↑ Barth ML, Fensom A, Harris A. Prevalence of common mutations in the arylsulphatase A gene in metachromatic leukodystrophy patients diagnosed in Britain. Hum Genet. 1993 Mar;91(1):73-7. PMID:8095918
  8. ↑ Honke K, Kobayashi T, Fujii T, Gasa S, Xu M, Takamaru Y, Kondo R, Tsuji S, Makita A. An adult-type metachromatic leukodystrophy caused by substitution of serine for glycine-122 in arylsulfatase A. Hum Genet. 1993 Nov;92(5):451-6. PMID:7902317
  9. ↑ Barth ML, Fensom A, Harris A. Missense mutations in the arylsulphatase A genes of metachromatic leukodystrophy patients. Hum Mol Genet. 1993 Dec;2(12):2117-21. PMID:7906588
  10. ↑ Harvey JS, Nelson PV, Carey WF, Robertson EF, Morris CP. An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy. Hum Mutat. 1993;2(4):261-7. PMID:8104633 doi:http://dx.doi.org/10.1002/humu.1380020405
  11. ↑ Hasegawa Y, Kawame H, Ida H, Ohashi T, Eto Y. Single exon mutation in arylsulfatase A gene has two effects: loss of enzyme activity and aberrant splicing. Hum Genet. 1994 Apr;93(4):415-20. PMID:7909527
  12. ↑ Heinisch U, Zlotogora J, Kafert S, Gieselmann V. Multiple mutations are responsible for the high frequency of metachromatic leukodystrophy in a small geographic area. Am J Hum Genet. 1995 Jan;56(1):51-7. PMID:7825603
  13. ↑ Kafert S, Heinisch U, Zlotogora J, Gieselmann V. A missense mutation P136L in the arylsulfatase A gene causes instability and loss of activity of the mutant enzyme. Hum Genet. 1995 Feb;95(2):201-4. PMID:7860068
  14. ↑ Barth ML, Fensom A, Harris A. Identification of seven novel mutations associated with metachromatic leukodystrophy. Hum Mutat. 1995;6(2):170-6. PMID:7581401 doi:http://dx.doi.org/10.1002/humu.1380060210
  15. ↑ Tsuda T, Hasegawa Y, Eto Y. Two novel mutations in a Japanese patient with the late-infantile form of metachromatic leukodystrophy. Brain Dev. 1996 Sep-Oct;18(5):400-3. PMID:8891236
  16. ↑ Regis S, Filocamo M, Stroppiano M, Corsolini F, Gatti R. A T > C transition causing a Leu > Pro substitution in a conserved region of the arylsulfatase A gene in a late infantile metachromatic leukodystrophy patient. Clin Genet. 1997 Jul;52(1):65-7. PMID:9272717
  17. ↑ Draghia R, Letourneur F, Drugan C, Manicom J, Blanchot C, Kahn A, Poenaru L, Caillaud C. Metachromatic leukodystrophy: identification of the first deletion in exon 1 and of nine novel point mutations in the arylsulfatase A gene. Hum Mutat. 1997;9(3):234-42. PMID:9090526 doi:<234::AID-HUMU4>3.0.CO;2-7 10.1002/(SICI)1098-1004(1997)9:3<234::AID-HUMU4>3.0.CO;2-7
  18. ↑ Regis S, Filocamo M, Stroppiano M, Corsolini F, Caroli F, Gatti R. A 9-bp deletion (2320del9) on the background of the arylsulfatase A pseudodeficiency allele in a metachromatic leukodystrophy patient and in a patient with nonprogressive neurological symptoms. Hum Genet. 1998 Jan;102(1):50-3. PMID:9490297
  19. ↑ Gomez-Lira M, Perusi C, Mottes M, Pignatti PF, Manfredi M, Rizzuto N, Salviati A. Molecular genetic characterization of two metachromatic leukodystrophy patients who carry the T799G mutation and show different phenotypes; description of a novel null-type mutation. Hum Genet. 1998 Apr;102(4):459-63. PMID:9600244
  20. ↑ Coulter-Mackie MB, Gagnier L. Two novel mutations in the arylsulfatase A gene associated with juvenile (R390Q) and adult onset (H397Y) metachromatic leukodystrophy. Hum Mutat. 1998;Suppl 1:S254-6. PMID:9452102
  21. ↑ Kurosawa K, Ida H, Eto Y. Prevalence of arylsulphatase A mutations in 11 Japanese patients with metachromatic leukodystrophy: identification of two novel mutations. J Inherit Metab Dis. 1998 Oct;21(7):781-2. PMID:9819708
  22. ↑ Marcao A, Amaral O, Pinto E, Pinto R, Sa Miranda MC. Metachromatic leucodystrophy in Portugal-finding of four new molecular lesions: C300F, P425T, g.1190-1191insC, and g.2408delC. Mutations in brief no. 232. Online. Hum Mutat. 1999;13(4):337-8. PMID:10220151 doi:<337::AID-HUMU12>3.0.CO;2-F 10.1002/(SICI)1098-1004(1999)13:4<337::AID-HUMU12>3.0.CO;2-F
  23. ↑ Gort L, Coll MJ, Chabas A. Identification of 12 novel mutations and two new polymorphisms in the arylsulfatase A gene: haplotype and genotype-phenotype correlation studies in Spanish metachromatic leukodystrophy patients. Hum Mutat. 1999;14(3):240-8. PMID:10477432 doi:<240::AID-HUMU7>3.0.CO;2-L 10.1002/(SICI)1098-1004(1999)14:3<240::AID-HUMU7>3.0.CO;2-L
  24. ↑ Halsall DJ, Halligan EP, Elsey TS, Cox TM. Metachromatic leucodystrophy: a newly identified mutation in arylsulphatase A, D281Y, found as a compound heterozygote with I179L in an adult onset case. Hum Mutat. 1999 Nov;14(5):447. PMID:10533072 doi:<447::AID-HUMU12>3.0.CO;2-1 10.1002/(SICI)1098-1004(199911)14:5<447::AID-HUMU12>3.0.CO;2-1
  25. ↑ Qu Y, Shapira E, Desnick RJ. Metachromatic leukodystrophy: subtype genotype/phenotype correlations and identification of novel missense mutations (P148L and P191T) causing the juvenile-onset disease. Mol Genet Metab. 1999 Jul;67(3):206-12. PMID:10381328 doi:10.1006/mgme.1999.2865
  26. ↑ Hermann S, Schestag F, Polten A, Kafert S, Penzien J, Zlotogora J, Baumann N, Gieselmann V. Characterization of four arylsulfatase A missense mutations G86D, Y201C, D255H, and E312D causing metachromatic leukodystrophy. Am J Med Genet. 2000 Mar 6;91(1):68-73. PMID:10751093
  27. ↑ Felice KJ, Gomez Lira M, Natowicz M, Grunnet ML, Tsongalis GJ, Sima AA, Kaplan RF. Adult-onset MLD: a gene mutation with isolated polyneuropathy. Neurology. 2000 Oct 10;55(7):1036-9. PMID:11061266
  28. ↑ Arbour LT, Silver K, Hechtman P, Treacy EP, Coulter-Mackie MB. Variable onset of metachromatic leukodystrophy in a Vietnamese family. Pediatr Neurol. 2000 Aug;23(2):173-6. PMID:11020646
  29. ↑ Comabella M, Waye JS, Raguer N, Eng B, Dominguez C, Navarro C, Borras C, Krivit W, Montalban X. Late-onset metachromatic leukodystrophy clinically presenting as isolated peripheral neuropathy: compound heterozygosity for the IVS2+1G-->A mutation and a newly identified missense mutation (Thr408Ile) in a Spanish family. Ann Neurol. 2001 Jul;50(1):108-12. PMID:11456299
  30. ↑ Regis S, Corsolini F, Stroppiano M, Cusano R, Filocamo M. Contribution of arylsulfatase A mutations located on the same allele to enzyme activity reduction and metachromatic leukodystrophy severity. Hum Genet. 2002 Apr;110(4):351-5. Epub 2002 Mar 8. PMID:11941485 doi:10.1007/s00439-002-0701-y
  31. ↑ Marcao A, Simonis H, Schestag F, Sa Miranda MC, Gieselmann V. Biochemical characterization of two (C300F, P425T) arylsulfatase a missense mutations. Am J Med Genet A. 2003 Jan 30;116A(3):238-42. PMID:12503099 doi:10.1002/ajmg.a.10822
  32. ↑ Marcao A, Azevedo JE, Gieselmann V, Sa Miranda MC. Oligomerization capacity of two arylsulfatase A mutants: C300F and P425T. Biochem Biophys Res Commun. 2003 Jun 20;306(1):293-7. PMID:12788103
  33. ↑ Eng B, Nakamura LN, O'Reilly N, Schokman N, Nowaczyk MM, Krivit W, Waye JS. Identification of nine novel arylsulfatase a (ARSA) gene mutations in patients with metachromatic leukodystrophy (MLD). Hum Mutat. 2003 Nov;22(5):418-9. PMID:14517960 doi:10.1002/humu.9190
  34. ↑ Olkhovich NV, Takamura N, Pichkur NA, Gorovenko NG, Aoyagi K, Yamashita S. Novel mutations in arylsulfatase A gene in three Ukrainian families with metachromatic leukodystrophy. Mol Genet Metab. 2003 Nov;80(3):360-3. PMID:14680985 doi:10.1016/j.ymgme.2003.08.004
  35. ↑ Berna L, Gieselmann V, Poupetova H, Hrebicek M, Elleder M, Ledvinova J. Novel mutations associated with metachromatic leukodystrophy: phenotype and expression studies in nine Czech and Slovak patients. Am J Med Genet A. 2004 Sep 1;129A(3):277-81. PMID:15326627 doi:10.1002/ajmg.a.30118
  36. ↑ Gallo S, Randi D, Bertelli M, Salviati A, Pandolfo M. Late onset MLD with normal nerve conduction associated with two novel missense mutations in the ASA gene. J Neurol Neurosurg Psychiatry. 2004 Apr;75(4):655-7. PMID:15026521
  37. ↑ Marcao AM, Wiest R, Schindler K, Wiesmann U, Weis J, Schroth G, Miranda MC, Sturzenegger M, Gieselmann V. Adult onset metachromatic leukodystrophy without electroclinical peripheral nervous system involvement: a new mutation in the ARSA gene. Arch Neurol. 2005 Feb;62(2):309-13. PMID:15710861 doi:10.1001/archneur.62.2.309
  38. ↑ Grossi S, Regis S, Rosano C, Corsolini F, Uziel G, Sessa M, Di Rocco M, Parenti G, Deodato F, Leuzzi V, Biancheri R, Filocamo M. Molecular analysis of ARSA and PSAP genes in twenty-one Italian patients with metachromatic leukodystrophy: identification and functional characterization of 11 novel ARSA alleles. Hum Mutat. 2008 Nov;29(11):E220-30. doi: 10.1002/humu.20851. PMID:18693274 doi:10.1002/humu.20851
  39. ↑ Cesani M, Capotondo A, Plati T, Sergi LS, Fumagalli F, Roncarolo MG, Naldini L, Comi G, Sessa M, Biffi A. Characterization of new arylsulfatase A gene mutations reinforces genotype-phenotype correlation in metachromatic leukodystrophy. Hum Mutat. 2009 Oct;30(10):E936-45. doi: 10.1002/humu.21093. PMID:19606494 doi:10.1002/humu.21093
  40. ↑ Lugowska A, Ploski R, Wlodarski P, Tylki-Szymanska A. Molecular bases of metachromatic leukodystrophy in Polish patients. J Hum Genet. 2010 Jun;55(6):394-6. doi: 10.1038/jhg.2010.25. Epub 2010 Mar 26. PMID:20339381 doi:10.1038/jhg.2010.25
  41. ↑ Hayashi T, Nakamura M, Ichiba M, Matsuda M, Kato M, Shiokawa N, Shimo H, Tomiyasu A, Mori S, Tomiyasu Y, Ishizuka T, Inamori Y, Okamoto Y, Umehara F, Arimura K, Nakabeppu Y, Sano A. Adult-type metachromatic leukodystrophy with compound heterozygous ARSA mutations: a case report and phenotypic comparison with a previously reported case. Psychiatry Clin Neurosci. 2011 Feb;65(1):105-8. doi:, 10.1111/j.1440-1819.2010.02169.x. PMID:21265945 doi:10.1111/j.1440-1819.2010.02169.x
  42. ↑ Schmidt B, Selmer T, Ingendoh A, von Figura K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. PMID:7628016
  43. ↑ Cosma MP, Pepe S, Parenti G, Settembre C, Annunziata I, Wade-Martins R, Di Domenico C, Di Natale P, Mankad A, Cox B, Uziel G, Mancini GM, Zammarchi E, Donati MA, Kleijer WJ, Filocamo M, Carrozzo R, Carella M, Ballabio A. Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency. Hum Mutat. 2004 Jun;23(6):576-81. PMID:15146462 doi:10.1002/humu.20040

1auk, resolution 2.10Å

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