AGXT

AGXT
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 1H0C, 1J04, 2YOB, 3R9A, 4CBR, 4CBS, 4I8A, 4KXK, 4KYO
Identifikatori
Aliasi	AGXT
Vanjski ID-jevi	OMIM: 604285 MGI: 1329033 HomoloGene: 37251 GeneCards: AGXT
EC broj	2.6.1.44
Lokacija gena (čovjek) Hrom. Hromosom 2 (čovjek) Bend 2q37.3 Početak 240,868,824 bp Kraj 240,880,502 bp
Lokacija gena (miš) Hrom. Hromosom 1 (miš) Bend 1 D|1 47.0 cM Početak 93,062,962 bp Kraj 93,073,143 bp
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • aktivnost sa transferazom • protein homodimerization activity • amino acid binding • alanine-glyoxylate transaminase activity • serine-pyruvate transaminase activity • transaminase activity • protein self-association • catalytic activity • GO:0001948, GO:0016582 vezivanje za proteine • pyridoxal phosphate binding • signaling receptor binding • vezivanje identičnih proteina Ćelijska komponenta • Peroksisom • mitochondrial matrix • peroxisomal matrix • mitohondrija • intracellular membrane-bounded organelle • citosol Biološki proces • Notch signaling pathway • oxalic acid secretion • glyoxylate catabolic process • glycine biosynthetic process, by transamination of glyoxylate • pyruvate biosynthetic process • L-alanine catabolic process • response to glucocorticoid • response to cAMP • L-cysteine catabolic process • cellular nitrogen compound metabolic process • glyoxylate metabolic process • protein targeting to peroxisome Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	189	11611
Ensembl	ENSG00000172482	ENSMUSG00000026272
UniProt	P21549	O35423
RefSeq (mRNK)	NM_000030	NM_001276710 NM_016702
RefSeq (bjelančevina)	NP_000021	NP_001263639 NP_057911
Lokacija (UCSC)	Chr 2: 240.87 – 240.88 Mb	Chr 1: 93.06 – 93.07 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Serin—piruvat aminotransferaza jest enzim koji je kod ljudi kodiran genom AGXT sa hromosoma 2.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 392 aminokiseline, a molekulska težina 43.010 Da.

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MASHKLLVTP		PKALLKPLSI		PNQLLLGPGP		SNLPPRIMAA		GGLQMIGSMS
KDMYQIMDEI		KEGIQYVFQT		RNPLTLVISG		SGHCALEAAL		VNVLEPGDSF
LVGANGIWGQ		RAVDIGERIG		ARVHPMTKDP		GGHYTLQEVE		EGLAQHKPVL
LFLTHGESST		GVLQPLDGFG		ELCHRYKCLL		LVDSVASLGG		TPLYMDRQGI
DILYSGSQKA		LNAPPGTSLI		SFSDKAKKKM		YSRKTKPFSF		YLDIKWLANF
WGCDDQPRMY		HHTIPVISLY		SLRESLALIA		EQGLENSWRQ		HREAAAYLHG
RLQALGLQLF		VKDPALRLPT		VTTVAVPAGY		DWRDIVSYVI		DHFDIEIMGG
LGPSTGKVLR		IGLLGCNATR		ENVDRVTEAL		RAALQHCPKK		KL

Funkcija

Ovaj gen je eksprimiran samo u jetri, a kodirani protein je uglavnom lokaliziran u peroksisomima, gdje je uključen u detoksikaciju gliokzilata. Mutacije ovog gena, od kojih neke mijenjaju subćelijsko ciljanje, povezane su sa primarnom tipom I hiperoksalurije.

Također pogledajte

• Peroksisomski poremećaj

Dopunska literatura

• Danpure CJ (1993). "Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase". Biochimie. 75 (3–4): 309–15. doi:10.1016/0300-9084(93)90091-6. PMID 8507692.
• Danpure CJ (2005). "Molecular etiology of primary hyperoxaluria type 1: new directions for treatment". Am. J. Nephrol. 25 (3): 303–10. doi:10.1159/000086362. PMID 15961951.
• Minatogawa Y, Tone S, Allsop J, et al. (1993). "A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1". Hum. Mol. Genet. 1 (8): 643–4. doi:10.1093/hmg/1.8.643. PMID 1301173.
• Purdue PE, Lumb MJ, Allsop J, et al. (1992). "A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1". Genomics. 13 (1): 215–8. doi:10.1016/0888-7543(92)90225-H. PMID 1349575.
• Purdue PE, Takada Y, Danpure CJ (1991). "Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1". J. Cell Biol. 111 (6 Pt 1): 2341–51. doi:10.1083/jcb.111.6.2341. PMC 2116406. PMID 1703535.
• Purdue PE, Allsop J, Isaya G, et al. (1992). "Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10900–4. doi:10.1073/pnas.88.23.10900. PMC 53039. PMID 1961759.
• Nishiyama K, Berstein G, Oda T, Ichiyama A (1991). "Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase". Eur. J. Biochem. 194 (1): 9–18. doi:10.1111/j.1432-1033.1990.tb19420.x. hdl:10271/960. PMID 2253628.
• Takada Y, Kaneko N, Esumi H, et al. (1990). "Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon". Biochem. J. 268 (2): 517–20. doi:10.1042/bj2680517. PMC 1131464. PMID 2363689.
• Danpure CJ, Jennings PR (1986). "Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I". FEBS Lett. 201 (1): 20–4. doi:10.1016/0014-5793(86)80563-4. PMID 3709805. S2CID 32933133.
• Danpure CJ, Fryer P, Jennings PR, et al. (1995). "Evolution of alanine:glyoxylate aminotransferase 1 peroxisomal and mitochondrial targeting. A survey of its subcellular distribution in the livers of various representatives of the classes Mammalia, Aves and Amphibia". Eur. J. Cell Biol. 64 (2): 295–313. PMID 7813517.
• Danpure CJ, Purdue PE, Fryer P, et al. (1993). "Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation". Am. J. Hum. Genet. 53 (2): 417–32. PMC 1682352. PMID 8101040.
• Minatogawa Y, Kawai C, Hatada S, Sato M (1997). "Liver specific kynurenine(alanine):glyoxylate aminotransferase was expressed in kidney cell line". Adv. Exp. Med. Biol. 398: 471–6. doi:10.1007/978-1-4613-0381-7_73. PMID 8906307.
• von Schnakenburg C, Rumsby G (1997). "Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene". J. Med. Genet. 34 (6): 489–92. doi:10.1136/jmg.34.6.489. PMC 1050973. PMID 9192270.
• Amoroso A, Pirulli D, Puzzer D, et al. (1999). "Gene symbol: AGXT. Disease: primary hyperoxaluria type I". Hum. Genet. 104 (5): 441. doi:10.1007/s004390050984. PMID 10394939. S2CID 34307977.
• Pirulli D, Puzzer D, Ferri L, et al. (1999). "Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene". Hum. Genet. 104 (6): 523–5. doi:10.1007/s004390050998. PMID 10453743. S2CID 28076033.
• Basmaison O, Rolland MO, Cochat P, Bozon D (2000). "Identification of 5 novel mutations in the AGXT gene". Hum. Mutat. 15 (6): 577. doi:10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-#. PMID 10862087.
• Lumb MJ, Danpure CJ (2000). "Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations". J. Biol. Chem. 275 (46): 36415–22. doi:10.1074/jbc.M006693200. PMID 10960483.

Vanjski linkovi

• GeneReviews/NIH/NCBI/UW entry on Primary Hyperoxaluria Type 1

• Lokacija ljudskog genoma AGT i stranica sa detaljima o genu AGT u UCSC Genome Browseru.
• Lokacija ljudskog genoma AGXT i stranica sa detaljima o genu AGXT u UCSC Genome Browseru.