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PMC	članci
PubMed	članci
NCBI	proteini

Glicin N-metiltransferaza
Glicin N-metiltransferaza
Identifikatori
EC broj	2.1.1.20
CAS broj	37228-72-1
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Glicin N-metiltransferaza (EC 2.1.1.20, glicinska metiltransferaza, S-adenozil-L-metionin:glicin metiltransferaza, GNMT) je enzim sa sistematskim imenom S-adenozil-L-metionin:glicin N-metiltransferaza.^[1]^[2]^[3]^[4]^[5]^[6] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + glicin

\rightleftharpoons

S-adenozil-L-homocistein + sarkozin

Ovaj enzim učestvuje u regulaciji metabolizma metil grupe u jetri i pankreasu putem regulacije odnosa između S-adenozil-L-metionina i S-adenozil-L-homocisteina.

Reference

^ Blumenstein, J. & Williams, G.R. (1963). „Glycine methyltransferase”. Can. J. Biochem. Physiol. 41: 201—210. PMID 13971907.
^ Ogawa, H., Gomi, T., Takusagawa, F. and Fujioka, M. (1998). „Structure, function and physiological role of glycine N-methyltransferase”. Int. J. Biochem. Cell Biol. 30: 13—26. PMID 9597750.
^ Yeo, E.J., Briggs, W.T. and Wagner, C. (1999). „Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate”. J. Biol. Chem. 274: 37559—37564. PMID 10608809.
^ Martinov, M.V., Vitvitsky, V.M., Mosharov, E.V., Banerjee, R. and Ataullakhanov, F.I. (2000). „A substrate switch: a new mode of regulation in the methionine metabolic pathway”. J. Theor. Biol. 204: 521—532. PMID 10833353.
^ Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. and Takusagawa, F. (2003). „Catalytic mechanism of glycine N-methyltransferase”. Biochemistry. 42: 8394—8402. PMID 12859184.
^ Pakhomova, S., Luka, Z., Grohmann, S., Wagner, C. and Newcomer, M.E. (2004). „Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes”. Proteins. 57: 331—337. PMID 15340920.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Glycine+N-methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Blumenstein, J. & Williams, G.R. (1963). „Glycine methyltransferase”. Can. J. Biochem. Physiol. 41: 201—210. PMID 13971907.

[2] Ogawa, H., Gomi, T., Takusagawa, F. and Fujioka, M. (1998). „Structure, function and physiological role of glycine N-methyltransferase”. Int. J. Biochem. Cell Biol. 30: 13—26. PMID 9597750.

[3] Yeo, E.J., Briggs, W.T. and Wagner, C. (1999). „Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate”. J. Biol. Chem. 274: 37559—37564. PMID 10608809.

[4] Martinov, M.V., Vitvitsky, V.M., Mosharov, E.V., Banerjee, R. and Ataullakhanov, F.I. (2000). „A substrate switch: a new mode of regulation in the methionine metabolic pathway”. J. Theor. Biol. 204: 521—532. PMID 10833353.

[5] Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. and Takusagawa, F. (2003). „Catalytic mechanism of glycine N-methyltransferase”. Biochemistry. 42: 8394—8402. PMID 12859184.

[6] Pakhomova, S., Luka, Z., Grohmann, S., Wagner, C. and Newcomer, M.E. (2004). „Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes”. Proteins. 57: 331—337. PMID 15340920.

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