L-gulonolakton oksidaza
L-gulonolakton oksidaza (EC 1.1.3.8) je enzim koji katalizuje reakciju D-glukuronolaktona (L-gulono-1,4-lakton) sa kiseonikom do L-ksilo-heks-3-gulonolaktona i vodonik peroksida. On koristi FAD kao kofaktor. L-ksilo-heks-3-gulonolakton (2-keto-gulono-gama-lakton) ima sposobnost spontanog konvertovanja u heksuronsku kiselinu (askorbinsku kiselinu), bez enzimskog posredovanja.
| L-gulonolakton oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.3.8 | ||||||||
| CAS broj | 9028-78-8 | ||||||||
| 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 | ||||||||
| Ontologija gena | AmiGO / EGO | ||||||||
| |||||||||
| Gulonolakton (L-) oksidaza, pseudogen | |||||
|---|---|---|---|---|---|
| Identifikatori | |||||
| Simboli | GULOP; GULO; SCURVY | ||||
| Vanjski ID | OMIM: 240400 MGI: 1353434 GeneCards: GULOP Gene | ||||
| EC broj | 1.1.3.8 | ||||
| |||||
| Ortolozi | |||||
| Vrsta | Čovek | Miš | |||
| Entrez | 2989 | 268756 | |||
| Ensembl | ENSG00000234770 | ENSMUSG00000034450 | |||
| UniProt | n/a | P58710 | |||
| RefSeq (mRNA) | NG_001136 | NM_178747 | |||
| RefSeq (protein) | n/a | NP_848862 | |||
| Lokacija (UCSC) |
Chr 8: 27.49 - 27.5 Mb |
Chr 14: 66.61 - 66.63 Mb | |||
| PubMed pretraga | [1] | [2] | |||
Deficijencija gulonolakton oksidaze
уредиNefunkcionalni pseudogen gulonolakton oksidaza (GULOP) je mapiran na humanom hromozomu 8p21. On odgovara evoluciono konzerviranom segmentu na bilo hromozomu 4 (SSC4) ili 14 (SSC14) svinje.[1][2][3] GULO proizvodi prekurzor askorbinske kiseline, koji se spontano konvertuje do vitamina ("vitamina C").
Reference
уреди- ^ GULOP Архивирано на сајту Wayback Machine (27. септембар 2007) - iHOP
- ^ Nishikimi M, Koshizaka T, Ozawa T, Yagi K (1988). „Occurrence in humans and guinea pigs of the gene related to their missing enzyme L-gulono-gamma-lactone oxidase”. Arch. Biochem. Biophys. 267 (2): 842—6. PMID 3214183. doi:10.1016/0003-9861(88)90093-8.
- ^ Nishikimi M, Fukuyama R, Minoshima S, Shimizu N, Yagi K (1994). „Cloning and chromosomal mapping of the human nonfunctional gene for L-gulono-gamma-lactone oxidase, the enzyme for L-ascorbic acid biosynthesis missing in man”. J. Biol. Chem. 269 (18): 13685—8. PMID 8175804.
Literatura
уреди- Zhang ZD; Frankish A; Hunt T; et al. (2010). „Identification and analysis of unitary pseudogenes: historic and contemporary gene losses in humans and other primates.”. Genome biology. 11 (3): R26. PMID 20210993. doi:10.1186/gb-2010-11-3-r26.
- Inai Y, Ohta Y, Nishikimi M (2003). „The whole structure of the human nonfunctional L-gulono-gamma-lactone oxidase gene--the gene responsible for scurvy--and the evolution of repetitive sequences thereon.”. J. Nutr. Sci. Vitaminol. 49 (5): 315—9. PMID 14703305.
- Otowa T; Yoshida E; Sugaya N; et al. (2009). „Genome-wide association study of panic disorder in the Japanese population.”. J. Hum. Genet. 54 (2): 122—6. PMID 19165232. doi:10.1038/jhg.2008.17.
- 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.
