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Alkanal monooksigenaza (FMN-vezani)
Identifikatori
EC broj	1.14.14.3
CAS broj	9014-00-0
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Alkanal monooksigenaza (FMN-vezana) (EC 1.14.14.3, bakterijska luciferaza, aldehidna monooksigenaza, luciferaza, Vibrio fischeri luciferaza, alkanal,redukovani-FMN:kiseonik oksidoreduktaza (1-hidroksilacija, luminescencija), alkanal,FMNH₂:kiseonik oksidoreduktaza (1-hidroksilacija, luminescencija)) je enzim sa sistematskim imenom aldehid,FMNH₂:kiseonik oksidoreduktaza (1-hidroksilacija, luminescencija).^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

aldehid + FMNH₂ + O₂

\rightleftharpoons

karboksilat + FMN + H₂O + hnu

Reakciona sekvenca obuhvata inkorporaciju molekula kiseonika u redukovani FMN, i naknadnu reakcija sa aldehidom čime se formira aktivirani FMN.H₂O kompleks. Taj kompleks se razlaže emisijom svetla. Ovaj enzim je visoko specifičan za redukovani FMN, i za dugolančane alifatične aldehide sa osam ugljenika ili više.

Reference

↑ Hastings, J.W. (1978). „Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde”. Crit. Rev. Biochem. 5: 163-184. PMID 363350.
↑ Hastings, J.W. and Nealson, K.H. (1977). „Bacterial bioluminescence”. Annu. Rev. Microbiol. 31: 549-595. PMID 199107.
↑ Hastings, J.W. and Presswood, R.P. (1978). „Bacterial luciferase: FMNH₂-aldehyde oxidase”. Methods Enzymol. 53: 558-570. PMID 309549.
↑ Nealson, K.H. and Hastings, J.W. (1979). „Bacterial bioluminescence: its control and ecological significance”. Microbiol. Rev. 43: 496-518. PMID 396467.
↑ Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T. (1983). „O₂ incorporation into a long-chain fatty-acid during bacterial luminescence”. Biochim. Biophys. Acta 722: 297-301.

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 Alkanal+monooxygenase+(FMN)

[1] Hastings, J.W. (1978). „Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde”. Crit. Rev. Biochem. 5: 163-184. PMID 363350.

[2] Hastings, J.W. and Nealson, K.H. (1977). „Bacterial bioluminescence”. Annu. Rev. Microbiol. 31: 549-595. PMID 199107.

[3] Hastings, J.W. and Presswood, R.P. (1978). „Bacterial luciferase: FMNH₂-aldehyde oxidase”. Methods Enzymol. 53: 558-570. PMID 309549.

[4] Nealson, K.H. and Hastings, J.W. (1979). „Bacterial bioluminescence: its control and ecological significance”. Microbiol. Rev. 43: 496-518. PMID 396467.

[5] Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T. (1983). „O₂ incorporation into a long-chain fatty-acid during bacterial luminescence”. Biochim. Biophys. Acta 722: 297-301.

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