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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/02 16:22:45」(JST)

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Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate.^[1] In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase.^[2]

Biological background[edit]

As OPRTase is part of a bifunctional complex UMP synthase in humans, the function and stability of this enzyme is not necessarily directly associated with disorders in the human body. It is however reasonable to believe that a dysfunction in one of the enzymes will cause a dysfunction of the whole enzyme.^[3] Defects in UMP synthase is associated with hypochromic anemia. ^[3]

Protein structure and function[edit]

The crystal structure of OPRTase has been solved several times by various scientific groups. ^[1]^[4]^[5]^[6] The overall structure is a dimer of two subunits, each consisting of seven α-helices and ten β-strands. The active site can be closed by a flexible loop, that prevents solvent from entering during reaction. ^[1]

References[edit]

^ ^a ^b ^c ^d González-Segura L, Witte JF, McClard RW, Hurley TD (December 2007). "Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase". Biochemistry 46 (49): 14075–86. doi:10.1021/bi701023z. PMID 18020427.
^ Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW. (1996). "Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase.". J Biol Chem. 271 (18): 10704–10708. doi:10.1074/jbc.271.18.10704. PMID 8631878.
^ ^a ^b Musick DL. (1981). "Structural Features of the Phosphoribosyltransferases and Their Relationship to the Human Deficiency Disorders of Purine and Pyrimidine Metabolism.". Critical Reviews in Biochemistry and Molecular Biology 11 (June): 1–34.
^ Grubmeyer C, Hansen MR, Fedorov AA, Almo SC (2012). "Structure of Salmonella typhimurium OMP Synthase in a Complete Substrate Complex". Biochemistry 51: 4397–4405.
^ Henriksen A, Aghajari N, Jensen KF, Gajhede M (1996). "A Flexible Loop at the Dimer Interface Is a Part of the Active Site of the Adjacent Monomer of Escherichia Coli Orotate Phosphoribosyltransferase". Biochemistry 35 (12): 3803–3809.
^ Scapin G, Grubmeyer C, Sacchettini JC (1994). "Crystal Structure of Orotate Phosphoribosyltransferase". Biochemistry 33 (6): 1287–1294.

UpToDate Contents

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English Journal

Structure of Plasmodium falciparum orotate phosphoribosyltransferase with autologous inhibitory protein-protein interactions.

Kumar S1, Krishnamoorthy K1, Mudeppa DG1, Rathod PK1.
Acta crystallographica. Section F, Structural biology communications.Acta Crystallogr F Struct Biol Commun.2015 May;71(Pt 5):600-8. doi: 10.1107/S2053230X1500549X. Epub 2015 Apr 21.
The most severe form of malaria is caused by the obligate parasite Plasmodium falciparum. Orotate phosphoribosyltransferase (OPRTase) is the fifth enzyme in the de novo pyrimidine-synthesis pathway in the parasite, which lacks salvage pathways. Among all of the malaria de novo pyrimidine-biosynthesi
PMID 25945715

Accumulation of Pyrimidine Intermediate Orotate Decreases Virulence Factor Production in Pseudomonas aeruginosa.

Niazy A1, Hughes LE.
Current microbiology.Curr Microbiol.2015 Apr 28. [Epub ahead of print]
The impact of orotate accumulation in the medically important bacterium Pseudomonas aeruginosa was studied by deleting pyrE, the gene encoding orotate phosphoribosyltransferase and responsible for converting orotate into orotate monophosphate within the de novo pyrimidine synthesis pathway. The pyrE
PMID 25917504

Japanese Journal

口腔扁平上皮癌におけるフッ化ピリミジン系抗癌剤活性化酵素の発現と薬剤奏効性との関係

渡辺正人,里見貴史,松田憲一,續雅子,松尾朗,金子忠良,岩本宗春,千葉博茂
頭頸部癌 = Head and neck cancer 34(4), 498-502, 2008-12-25
NAID 10024931700

「オロチン酸ホスホリボシル転移酵素」

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NCBI	proteins

Orotate phosphoribosyltransferase
	; S. cerevisiae orotate phosphoribosyl transferase bound to its substrates. From PDB file 2PS1.
Identifiers
EC number	2.4.2.10
CAS number	9030-25-5
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
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PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: orotate phosphoribosyltransferase
関: オロチン酸ホスホリボシル基転移酵素、オロチン酸ホスホリボシルトランスフェラーゼ

「オロチン酸ホスホリボシル基転移酵素」

　　[★]

英: orotate phosphoribosyltransferase
関: オロチン酸ホスホリボシル転移酵素、オロチン酸ホスホリボシルトランスフェラーゼ

「オロチン酸ホスホリボシルトランスフェラーゼ」

　　[★]

英: orotate phosphoribosyltransferase
関: オロチン酸ホスホリボシル転移酵素、オロチン酸ホスホリボシル基転移酵素

「オロト酸ホスホリボシルトランスフェラーゼ」

　　[★]

英: [[]]
同: orotate phosphoribosyltransferase
関: [[]]

同: orotate phosphoribosyltransferase

「OPRT deficiency」

　　[★]

同: orotate phosphoribosyltransferase

「orotate」

　　[★]

オロト酸、オロチン酸、オロト酸塩、オロチン酸塩

関: orotic acid

orotic acid

「phosphoribosyltransferase」

　　[★] ホスホリボシルトランスフェラーゼ、ホスホリボシル基転移酵素

[name-1] González-Segura L, Witte JF, McClard RW, Hurley TD (December 2007). "Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase". Biochemistry 46 (49): 14075–86. doi:10.1021/bi701023z. PMID 18020427.

[2] Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW. (1996). "Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase.". J Biol Chem. 271 (18): 10704–10708. doi:10.1074/jbc.271.18.10704. PMID 8631878.

[Musick-3] Musick DL. (1981). "Structural Features of the Phosphoribosyltransferases and Their Relationship to the Human Deficiency Disorders of Purine and Pyrimidine Metabolism.". Critical Reviews in Biochemistry and Molecular Biology 11 (June): 1–34.

[Grubmeyer2012-4] Grubmeyer C, Hansen MR, Fedorov AA, Almo SC (2012). "Structure of Salmonella typhimurium OMP Synthase in a Complete Substrate Complex". Biochemistry 51: 4397–4405.

[Henriksen1996-5] Henriksen A, Aghajari N, Jensen KF, Gajhede M (1996). "A Flexible Loop at the Dimer Interface Is a Part of the Active Site of the Adjacent Monomer of Escherichia Coli Orotate Phosphoribosyltransferase". Biochemistry 35 (12): 3803–3809.

[Scapin1994-6] Scapin G, Grubmeyer C, Sacchettini JC (1994). "Crystal Structure of Orotate Phosphoribosyltransferase". Biochemistry 33 (6): 1287–1294.

リンク元	「オロチン酸ホスホリボシル転移酵素」「オロチン酸ホスホリボシル基転移酵素」「オロチン酸ホスホリボシルトランスフェラーゼ」「オロト酸ホスホリボシルトランスフェラーゼ」「OPRT deficiency」
関連記事	「orotate」「phosphoribosyltransferase」

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案内

orotate phosphoribosyltransferase