ウロポルフィリノーゲンIII合成酵素
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- the 9th letter of the Roman alphabet (同)i
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- iodineの化学記号
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/01/03 21:23:51」(JST)
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| Uroporphyrinogen-III synthase |
| Identifiers |
| EC number |
4.2.1.75 |
| CAS number |
37340-55-9 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI Protein |
search |
|
| Uroporphyrinogen III synthase |
| Identifiers |
| Symbol |
UROS |
| Entrez |
7390 |
| HUGO |
12592 |
| OMIM |
606938 |
| RefSeq |
NM_000375 |
| UniProt |
P10746 |
| Other data |
| EC number |
4.2.1.75 |
| Locus |
Chr. 10 q25.2-26.3 |
| Uroporphyrinogen-III synthase HemD |
|
| crystal structure of uroporphyrinogen iii synthase from an extremely thermophilic bacterium thermus thermophilus hb8 (wild type, native, form-2 crystal) |
| Identifiers |
| Symbol |
HEM4 |
| Pfam |
PF02602 |
| InterPro |
IPR003754 |
| SCOP |
1jr2 |
| SUPERFAMILY |
1jr2 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe |
| PDBsum |
structure summary |
|
Uroporphyrinogen III synthase EC 4.2.1.75 is an enzyme involved in the metabolism of the cyclic tetrapyrrole compound porphyrin. It is involved in the conversion of hydroxymethyl bilane into uroporphyrinogen III. This enzyme catalyses the inversion of the final pyrrole unit (ring D) of the linear tetrapyrrole molecule, linking it to the first pyrrole unit (ring A), thereby generating a large macrocyclic structure, uroporphyrinogen III.[1] The enzyme folds into two alpha/beta domains connected by a beta-ladder, the active site being located between the two domains.[2]
Heme synthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow)
Pathology
A deficiency is associated with Gunther's disease, also known as congenital erythropoietic porphyria (CEP). This is an autosomal recessive inborn error of metabolism that results from the markedly deficient activity of uroporphyrinogen III synthase .[3]
External links
- Uroporphyrinogen+III+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
References
- ^ Raux E, Schubert HL, Warren MJ (December 2000). "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum". Cell. Mol. Life Sci. 57 (13-14): 1880–93. doi:10.1007/PL00000670. PMID 11215515.
- ^ Mathews MA, Schubert HL, Whitby FG, Alexander KJ, Schadick K, Bergonia HA, Phillips JD, Hill CP (November 2001). "Crystal structure of human uroporphyrinogen III synthase". EMBO J. 20 (21): 5832–9. doi:10.1093/emboj/20.21.5832. PMC 125291. PMID 11689424. //www.ncbi.nlm.nih.gov/pmc/articles/PMC125291/.
- ^ To-Figueras J, Badenas C, Mascaro JM, Madrigal I, Merino A, Bastida P, Lecha M, Herrero C (2007). "Study of the genotype-phenotype relationship in four cases of congenital erythropoietic porphyria". Blood Cells Mol. Dis. 38 (3): 242–6. doi:10.1016/j.bcmd.2006.12.001. PMID 17270473.
|
Metabolism: amino acid metabolism · porphyrin/heme enzymes
|
|
| Porphyrin biosynthesis |
early mitochondrial: Aminolevulinic acid synthase (ALAS1, ALAS2) · Porphobilinogen synthase
cytosolic: Porphobilinogen deaminase · Uroporphyrinogen III synthase · Uroporphyrinogen III decarboxylase · Coproporphyrinogen III oxidase
late mitochondrial: Protoporphyrinogen oxidase · Ferrochelatase
|
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Heme degradation
to bile |
spleen: Heme oxygenase · Biliverdin reductase
liver: glucuronosyltransferase (UGT1A1)
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
|
k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
|
m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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|
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cell/phys (coag, heme, immu, gran), csfs
|
rbmg/mogr/tumr/hist, sysi/epon, btst
|
drug (B1/2/3+5+6), btst, trns
|
|
|
|
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Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)
|
|
| 4.2.1: Hydro-Lyases |
- Carbonic anhydrase
- Fumarase
- Aconitase
- Enolase
- Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase
- Methylglutaconyl-CoA hydratase
- Tryptophan synthase
- Cystathionine beta synthase
- Porphobilinogen synthase
- 3-isopropylmalate dehydratase
- Urocanate hydratase
- Uroporphyrinogen III synthase
- Nitrile hydratase
|
|
| 4.2.2: Acting on polysaccharides |
|
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| 4.2.3: Acting on phosphates |
|
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| 4.2.99: Other |
- Carboxymethyloxysuccinate lyase
|
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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This article incorporates text from the public domain Pfam and InterPro IPR003754
UpToDate Contents
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English Journal
- Acquired erythropoietic uroporphyria secondary to myelodysplastic syndrome with chromosome 3 alterations. A case report.
- Podlipnik S1, Guijarro F2, Combalia A1, To-Figueras J3, Badenas C3, Costa D4, Rozman M4, Jorge S2, Aguilera P1, Gaya A2.
- The British journal of dermatology.Br J Dermatol.2017 Sep 2. doi: 10.1111/bjd.15927. [Epub ahead of print]
- PMID 28865079
- Impact of somatic copy number alterations on the glioblastoma miRNome: miR-4484 is a genomically deleted tumour suppressor.
- Nawaz Z1, Patil V1, Thinagararjan S1, Rao SA1, Hegde AS2, Arivazhagan A3, Santosh V4, Somasundaram K1.
- Molecular oncology.Mol Oncol.2017 Aug;11(8):927-944. doi: 10.1002/1878-0261.12060. Epub 2017 May 24.
- PMID 28378523
- Missense UROS mutations causing congenital erythropoietic porphyria reduce UROS homeostasis that can be rescued by proteasome inhibition.
- Blouin JM1,2,3, Bernardo-Seisdedos G4, Sasso E1,2,3, Esteve J1,2,3, Ged C1,2,3, Lalanne M1,2,3, Sanz-Parra A4, Urquiza P4, de Verneuil H1,2,3, Millet O4, Richard E1,2,3.
- Human molecular genetics.Hum Mol Genet.2017 Apr 15;26(8):1565-1576. doi: 10.1093/hmg/ddx067.
- PMID 28334762
Japanese Journal
- Purification and Characterization of Human Uroporphyrinogen III Synthase Expressed in Escherichia coli
- Purification and Characterization of Human Uroporphyrinogen III Synthase Expressed in <i>Escherichia coli</i>
- Human uroporphyrinogen-III synthase : genomic organization, alternative promoters, and erythroid-specific expression
Related Links
- The UROS gene provides instructions for making an enzyme known as uroporphyrinogen III synthase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs ...
- The protein encoded by this gene catalyzes the fourth step of porphyrin biosynthesis in the heme biosynthetic pathway. Defects in this gene cause congenital erythropoietic porphyria (Gunther's disease). [provided by RefSeq, Jul 2008]
★リンクテーブル★
[★]
- 英
- heme
- 同
- プロトヘム protoheme、フェロプロトポルフィリンIX ferroprotoporphyrin IX
- 関
- ヘマチン hematin
生合成
生合成の場所
[★]
- 英
- hydroxymethylbilane, HMB
- 関
- ビルフィリン症、ヘム
[★]
- 関
- uroporphyrinogen III synthase
- 同
- UROS
[★]
- 関
- lyase、synthetase、transferase
[★]
[★]
[★]
ウロ・ルフィリノーゲン
- 同
- uroporphyrinogens