Fosfoglicerat kinaza

Fosfoglocerat kinaza 1
Identifikatori
Simbol	PGK1
Entrez	5230
Hugo	8896
OMIM	311800
RefSek	NM_000291
UniProt	P00558
Drugi podaci
EC broj	2.7.2.3
Lokus	Hrom. X q13.3

Fosfoglicerat kinaza
	Struktura kvašćane fosfoglicerat kinaze.
Identifikatori
Simbol	PGK
Pfam	PF00162
InterPro	IPR001576
SKOP	3pgk
Dostupne PDB strukture:
13pk, 16pk, 1fw8, 1hdi, 1kf0, 1ltk, 1php, 1qpg, 1v6s, 1vjc, 1vjd, 1vpe, 1zmr, 2p9q, 2p9t, 2paa, 2zgv, 3c39, 3c3a, 3c3b, 3c3c, 3pgk

Fosfoglicerat kinaza
Identifikatori
EC broj	2.7.2.3
CAS broj	9001-83-6
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Ontologija gena	AmiGO / EGO
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Fosfoglicerat kinaza (EC 2.7.2.3) (PGK) je enzim koji katalizuje reverzibilni transfer fosfatne grupe sa ATP-a na 3-fosfoglicerat proizvodeći ADP i 1,3-bisfosfoglicerat. Popout svih kinaza PGK je transferaza. Glukoneogeneza i Kalvinov ciklus, koji su anabolički putevi, koriste ATP i vrše reakciju u suprotnom smeru. Glikoliza, katabolički put, koristi reverznu reakciju da proizvede ATP. Postoje varijante glikolize koje ne koriste PGK.

Mehanizam i struktura

Fosfoglicerat kinaza je prisutna u svim živim organizmima i njena sekvenca je visoko konzervirana tokom evolucije. Ovaj enzim je monomer koji sadrži dva domena približno jednake veličine koji odgovaraju N- i C-kraju proteina. 3-fosfoglicerat (3-PG) se vezuje za N-terminal, dok se nukleotidni supstrati, MgATP ili MgADP, vezuju za C-terminalni domen enzima.^[2] U osnovi svakog domena je šestolančana paralelna beta ravan okružena alfa heliksima. Domeni imaju sposobnost nezavisnog savijanja.^[3]^[4]

Ljudski izozimi

Fosfoglocerat kinaza 2
Identifikatori
Simbol	PGK2
Entrez	5232
Hugo	8898
OMIM	172270
RefSek	NM_138733
UniProt	P07205
Drugi podaci
EC broj	2.7.2.3
Lokus	Hrom. 6 p21-q12

Deficijencija fosfoglicerat kinaze (PGK) je vezana za hemolitičku anemiju i mentalne poremećaje kod ljudi.^[5]

References

↑ Watson HC, Walker NP, Shaw PJ, et al. (1982). „Sequence and structure of yeast phosphoglycerate kinase”. EMBO J. 1 (12): 1635–40. PMC 553262. PMID 6765200.
↑ Kumar S, Ma B, Tsai CJ, Wolfson H, Nussinov R (1999). „Folding funnels and conformational transitions via hinge-bending motions”. Cell Biochem. Biophys. 31 (2): 141–164. PMID 10593256.
↑ Yon JM, Desmadril M, Betton JM, Minard P, Ballery N, Missiakas D, Gaillard-Miran S, Perahia D, Mouawad L (1990). „Flexibility and folding of phosphoglycerate kinase”. Biochimie 72 (6-7): 417–429. PMID 2124145.
↑ Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M, Bowler MW (2011). „A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase”. J. Biol. Chem. 286 (16): 14040-8. DOI:10.1074/jbc.M110.206813. PMC 3077604. PMID 21349853.
↑ Yoshida A, Tani K (1983). „Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects”. Biomed. Biochim. Acta 42 (11-12): -. PMID 6689547.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Phosphoglycerate+kinase
Illustration at arizona.edu Arhivirano 2006-09-02 na Wayback Machine-u

[pmid6765200-1] Watson HC, Walker NP, Shaw PJ, et al. (1982). „Sequence and structure of yeast phosphoglycerate kinase”. EMBO J. 1 (12): 1635–40. PMC 553262. PMID 6765200.

[PUB00006511-2] Kumar S, Ma B, Tsai CJ, Wolfson H, Nussinov R (1999). „Folding funnels and conformational transitions via hinge-bending motions”. Cell Biochem. Biophys. 31 (2): 141–164. PMID 10593256.

[PUB00006255-3] Yon JM, Desmadril M, Betton JM, Minard P, Ballery N, Missiakas D, Gaillard-Miran S, Perahia D, Mouawad L (1990). „Flexibility and folding of phosphoglycerate kinase”. Biochimie 72 (6-7): 417–429. PMID 2124145.

[Zerrad11-4] Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M, Bowler MW (2011). „A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase”. J. Biol. Chem. 286 (16): 14040-8. DOI:10.1074/jbc.M110.206813. PMC 3077604. PMID 21349853.

[PUB00006482-5] Yoshida A, Tani K (1983). „Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects”. Biomed. Biochim. Acta 42 (11-12): -. PMID 6689547.

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p r u Proteini: enzimi
Teme	Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6