1e51: Difference between revisions

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~~[[Image:1e51.png|left|200px]]~~

===CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE===

==~~=CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE=~~==

==Disease==

[[http://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN]] Defects in ALAD are the cause of acute hepatic porphyria (AHEPP) [MIM:[http://omim.org/entry/612740 612740]]. A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralysis, and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.<ref>PMID:1569184</ref><ref>PMID:2063868</ref><ref>PMID:1309003</ref><ref>PMID:10706561</ref><ref>PMID:17236137</ref>

~~{{ABSTRACT_PUBMED_012794073}}~~

==Function==

[[http://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN]] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.<ref>PMID:11032836</ref><ref>PMID:19812033</ref>

==About this Structure==

[[1e51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E51 OCA].

==See Also==

*[[Porphobilinogen synthase|Porphobilinogen synthase]]

==Reference==

[[Category: Homo sapiens]]

[[Category: Porphobilinogen synthase]]

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@@ Line 1: / Line 1: @@
-[[Image:1e51.png|left|200px]]
 {{STRUCTURE_1e51|  PDB=1e51  |  SCENE=  }}
+===CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE===
+{{ABSTRACT_PUBMED_012794073}}
-===CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE===
+==Disease==
+[[http://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN]] Defects in ALAD are the cause of acute hepatic porphyria (AHEPP) [MIM:[http://omim.org/entry/612740 612740]]. A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralysis, and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.<ref>PMID:1569184</ref><ref>PMID:2063868</ref><ref>PMID:1309003</ref><ref>PMID:10706561</ref><ref>PMID:17236137</ref>
-{{ABSTRACT_PUBMED_012794073}}
+==Function==
+[[http://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN]] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.<ref>PMID:11032836</ref><ref>PMID:19812033</ref>
 ==About this Structure==
 [[1e51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E51 OCA].
+==See Also==
+*[[Porphobilinogen synthase|Porphobilinogen synthase]]
 ==Reference==
-<ref group="xtra">PMID:012897770</ref><references group="xtra"/>
+<ref group="xtra">PMID:012897770</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Porphobilinogen synthase]]