Amidaza

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Amidaza
Amidaza
Identifikatori
EC broj	3.5.1.4
CAS broj	9012-56-0
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

Amidaza (EC 3.5.1.4, acilamidaza, acilaza, amidohidrolaza, deaminaza, masna acilamidaza, N-acetilaminohidrolaza) je enzim sa sistematskim imenom acilamid amidohidrolaza.^[1]^[2] Ovaj enzim katalizuje sledeću hemijsku reakciju

Amid monokarboksilne kiseline + H₂O

\rightleftharpoons

monokarboksilat + NH₃

Reference

^ Bray, H.G., James, S.P., Raffan, I.M., Ryman, B.E. and Thorpe, W.V. (1949). „The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver”. Biochem. J. 44: 618—625. PMID 16748573.
^ Bray, H.G., James, S.P., Thorpe, W.V. and Wasdell, M.R. (1950). „The fate of certain organic acids and amides in the rabbit. 11. Further observations on the hydrolysis of amides by tissue extracts”. Biochem. J. 47: 294—299. PMID 14800883.

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

Amidase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Bray, H.G., James, S.P., Raffan, I.M., Ryman, B.E. and Thorpe, W.V. (1949). „The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver”. Biochem. J. 44: 618—625. PMID 16748573.

[2] Bray, H.G., James, S.P., Thorpe, W.V. and Wasdell, M.R. (1950). „The fate of certain organic acids and amides in the rabbit. 11. Further observations on the hydrolysis of amides by tissue extracts”. Biochem. J. 47: 294—299. PMID 14800883.

[1]

[2]

п р у Hidrolaze: ugljenično-azotne nepeptidne (EC 3.5)
3.5.1: Linearni amidi / Amidohidrolaze	Asparaginaza Glutaminaza Ureaza Biotinidaza Aspartoacilaza Keramidaza Aspartilglukozaminidaza Hidrolaza masno kiselinskih amida Histonska deacetilaza Sirtuin
3.5.2: Cyclic amides/ Amidohidrolaze	Barbituraza Beta-laktamaza
3.5.3: Linear amidines/ Ureohidrolaze	Arginaza Agmatinaza Protein-arginin deiminaza
3.5.4: Cyclic amidines/ Aminohidrolaze	Guanin deaminaza Adenozin deaminaza AMP deaminaza Inozin monofosfat sintaza DCMP deaminaza GTP ciklohidrolaza I Citidin deaminaza AICDA Aktivacijom indukovana citidinska deaminaza
3.5.5: Nitrili/ Aminohidrolaze	Nitrilaza
3.5.99: Drugi	Riboflavinaza Tiaminaza II

п р у Enzimi
Teme	Aktivno mesto Alosterna regulacija Mesto vezivanja Katalitički perfektan enzim Koenzim Kofaktor Kooperativnost EC broj Enzimska kataliza Inhibicija enzima Enzimska kinetika Lajnviver—Berkov dijagram Mihaelis—Mentenina 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