2aij: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2aij.png|left|200px]]
 {{STRUCTURE_2aij|  PDB=2aij  |  SCENE=  }}
+===Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide CTPSR===
+{{ABSTRACT_PUBMED_16368756}}
-===Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide CTPSR===
+==Disease==
+[[http://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN]] Defects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:[http://omim.org/entry/272200 272200]]. MSD is 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. Inheritance is autosomal recessive.<ref>PMID:12757706</ref><ref>PMID:12757705</ref><ref>PMID:15146462</ref><ref>PMID:18157819</ref> [[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>
-{{ABSTRACT_PUBMED_16368756}}
+==Function==
+[[http://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN]] Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.<ref>PMID:12757706</ref><ref>PMID:15657036</ref> [[http://www.uniprot.org/uniprot/ARSA_HUMAN ARSA_HUMAN]] Hydrolyzes cerebroside sulfate.
 ==About this Structure==
@@ Line 11: / Line 13: @@
 ==Reference==
-<ref group="xtra">PMID:016368756</ref><references group="xtra"/>
+<ref group="xtra">PMID:016368756</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Roeser, D.]]