PROFILPELAJAR.COM

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Triptofanska sintaza (spašavanje indola)
Triptofanska sintaza (spašavanje indola)
Identifikatori
EC broj	4.2.1.122
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

Triptofanska sintaza (spašavanje indola) (EC 4.2.1.122, triptofanska sintaza beta2) je enzim sa sistematskim imenom L-serin hidrolijaza (dodaje indol, formira L-triptofan).^[1] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-serin + indol

\rightleftharpoons

L-triptofan + H₂O

Ovaj enzim učestvuje u procesu spašavanja indola tokom formiranja L-triptofana.

Reference

^ Hettwer, S. & Sterner, R. (2002). „A novel tryptophan synthase β-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role”. J. Biol. Chem. 277: 8194—8201. PMID 11756459.

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

Tryptophan+synthase+(indole-salvaging) на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Hettwer, S. & Sterner, R. (2002). „A novel tryptophan synthase β-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role”. J. Biol. Chem. 277: 8194—8201. PMID 11756459.

[1]