グアニル酸キナーゼ

WordNet

an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/12/24 15:39:43」(JST)

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In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction

ATP + GMP ADP + GDP

Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism.

Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP.^[1] It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.^[2]^[3]^[4]

Nomenclature[edit]

The systematic name of this enzyme class is ATP:(d)GMP phosphotransferase. Other names in common use include"

deoxyguanylate kinase,
5'-GMP kinase,
GMP kinase,
guanosine monophosphate kinase, and
ATP:GMP phosphotransferase.

References[edit]

^ ^a ^b Stehle T, Schulz GE (April 1992). "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution". J. Mol. Biol. 224 (4): 1127–41. doi:10.1016/0022-2836(92)90474-X. PMID 1314905. Cite uses deprecated parameters (help)
^ Bryant PJ, Woods DF (February 1992). "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene". Cell 68 (4): 621–2. doi:10.1016/0092-8674(92)90136-Z. PMID 1310897. Cite uses deprecated parameters (help)
^ Zschocke PD, Schiltz E, Schulz GE (April 1993). "Purification and sequence determination of guanylate kinase from pig brain". Eur. J. Biochem. 213 (1): 263–9. doi:10.1111/j.1432-1033.1993.tb17757.x. PMID 8097461. Cite uses deprecated parameters (help)
^ Goebl MG (March 1992). "Is the erythrocyte protein p55 a membrane-bound guanylate kinase?". Trends Biochem. Sci. 17 (3): 99. doi:10.1016/0968-0004(92)90244-4. PMID 1329277. Cite uses deprecated parameters (help)

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English Journal

The mediation of platelet quiescence by NO-releasing polymers via cGMP-induced serine 239 phosphorylation of vasodilator-stimulated phosphoprotein.

Major TC, Handa H, Brisbois EJ, Reynolds MM, Annich GM, Meyerhoff ME, Bartlett RH.SourceDepartment of Surgery, University of Michigan Medical Center, Ann Arbor, MI, USA. Electronic address: tcmajor@umich.edu.
Biomaterials.Biomaterials.2013 Nov;34(33):8086-96. doi: 10.1016/j.biomaterials.2013.07.041. Epub 2013 Jul 29.
Nitric oxide (NO) releasing (NORel) materials have been shown to create localized increases in NO concentration by the release of NO from a diazeniumdiolate-containing or S-nitrosothiol-containing polymer coating and the improvement of extracorporeal circulation (ECC) hemocompatibility. However, the
PMID 23906514

MAGI-1 acts as a scaffolding molecule for NGF receptor-mediated signaling pathway.

Ito H, Morishita R, Iwamoto I, Mizuno M, Nagata K.SourceDepartment of Molecular Neurobiology, Institute for Developmental Research, Aichi Human Service Center, Kasugai, Aichi, Japan.
Biochimica et biophysica acta.Biochim Biophys Acta.2013 Oct;1833(10):2302-10. doi: 10.1016/j.bbamcr.2013.06.005. Epub 2013 Jun 13.
We have recently found that the membrane-associated guanylate kinase with inverted organization-1 (MAGI-1) was enriched in rat nervous tissues such as the glomeruli in olfactory bulb of adult rats and dorsal root entry zone in spinal cord of embryonic rats. In addition, we revealed the localization
PMID 23769981

What causes relapses of autoimmune diseases? The etiological role of autoreactive T cells.

Wildner G, Kaufmann U.SourceKlinikum der Universität München, Dept. of Ophthalmology, Mathildenstr. 8, 80336 Munich, Germany. Electronic address: Gerhild.Wildner@med.uni-muenchen.de.
Autoimmunity reviews.Autoimmun Rev.2013 Sep;12(11):1070-5. doi: 10.1016/j.autrev.2013.04.001. Epub 2013 May 16.
Most human autoimmune diseases have a relapsing-remitting or a chronic progressive course, while animal models are usually acute and monophasic. In our experimental animal model the disease can be either monophasic or remitting, depending on the autoantigen used for induction, and it appears to lie
PMID 23685277

Japanese Journal

Dlg5 interacts with the TGF-β receptor and promotes its degradation.

Sezaki Takuhito,Tomiyama Lucia,Kimura Yasuhisa,Ueda Kazumitsu,Kioka Noriyuki
FEBS letters 587(11), 1624-1629, 2013-06-05
… Discs large homolog 5 (Dlg5) is a member of the membrane-associated guanylate kinase adaptor family of proteins and is involved in epithelial-to-mesenchymal transition via transforming growth factor-β (TGF-β) signaling. …
NAID 120005293584

Role of Dlg5/lp-dlg, a Membrane-Associated Guanylate Kinase Family Protein, in Epithelial-Mesenchymal Transition in LLc-PK1 Renal Epithelial Cells.

Sezaki Takuhito,Inada Kohki,Sogabe Takayuki,Kakuda Kumiyo,Tomiyama Lucia,Matsuno Yohsuke,Ichikawa Takafumi,Matsuo Michinori,Ueda Kazumitsu,Kioka Noriyuki
PloS one 7(4), 2012-04-23
… Discs large homolog 5 (Dlg5) is a member of the membrane-associated guanylate kinase adaptor family of proteins, some of which are involved in the regulation of epithelial-to-mesenchymal transition (EMT). …
NAID 120004057187

Recent Progress in the Management of Pulmonary Hypertension

FUKUMOTO Yoshihiro,SHIMOKAWA Hiroaki
Circulation journal : official journal of the Japanese Circulation Society 75(8), 1801-1810, 2011-07-25
… Recently, significant progress has been made in the understanding of the pathophysiology, diagnosis and treatment of PH. Regarding the pathophysiology of the disorder, direct evidence for Rho-kinase activation in the pulmonary artery from PAH patients has been provided. …
NAID 10029127349

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「kinase」

guanylate kinase
	; Structure of Guanylate Kinase.
Identifiers
Symbol	Guanylate_kin
Pfam	PF00625
InterPro	IPR008144
PROSITE	PDOC00670
SCOP	1gky
SUPERFAMILY	1gky
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

guanylate kinase
Identifiers
EC number	2.7.4.8
CAS number	9026-59-9
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	proteins

　　[★] キナーゼカイネースリン酸化酵素 phosphoenzyme phosphotransferase 　

[pmid1314905-1] Stehle T, Schulz GE (April 1992). "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution". J. Mol. Biol. 224 (4): 1127–41. doi:10.1016/0022-2836(92)90474-X. PMID 1314905. Cite uses deprecated parameters (help)

[pmid1310897-2] Bryant PJ, Woods DF (February 1992). "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene". Cell 68 (4): 621–2. doi:10.1016/0092-8674(92)90136-Z. PMID 1310897. Cite uses deprecated parameters (help)

[pmid8097461-3] Zschocke PD, Schiltz E, Schulz GE (April 1993). "Purification and sequence determination of guanylate kinase from pig brain". Eur. J. Biochem. 213 (1): 263–9. doi:10.1111/j.1432-1033.1993.tb17757.x. PMID 8097461. Cite uses deprecated parameters (help)

[pmid1329277-4] Goebl MG (March 1992). "Is the erythrocyte protein p55 a membrane-bound guanylate kinase?". Trends Biochem. Sci. 17 (3): 99. doi:10.1016/0968-0004(92)90244-4. PMID 1329277. Cite uses deprecated parameters (help)

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guanylate kinase