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)
Kraj	240,880,502 bp
Lokacija gena (miš)
Hrom.	Hromosom 1 (miš)
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
	189
	11611
	ENSG00000172482
	ENSMUSG00000026272
	P21549
	O35423
	NM_000030
	NM_001276710; NM_016702
	NP_000021
	NP_001263639; NP_057911
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Serin—piruvat aminotransferaza jest enzim koji je kod ljudi kodiran genom AGXT sa hromosoma 2.^[5]^[6]^[7]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 392 aminokiseline, a molekulska težina 43.010 Da.^[8]

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.^[7]

Također pogledajte

Peroksisomski poremećaj

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000172482 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026272 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A (Jul 1991). "Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene". Biochem Biophys Res Commun. 176 (3): 1093–9. doi:10.1016/0006-291X(91)90396-O. PMID 2039493.
^ Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ (Jul 1991). "Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase". Genomics. 10 (1): 34–42. doi:10.1016/0888-7543(91)90481-S. PMID 2045108.
^ ^a ^b "Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)".
^ "UniProt, P21549" (jezik: engleski). Pristupljeno 15. 11. 2021.

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000172482 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026272 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2039493-5] Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A (Jul 1991). "Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene". Biochem Biophys Res Commun. 176 (3): 1093–9. doi:10.1016/0006-291X(91)90396-O. PMID 2039493.

[pmid2045108-6] Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ (Jul 1991). "Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase". Genomics. 10 (1): 34–42. doi:10.1016/0888-7543(91)90481-S. PMID 2045108.

[entrez-7] "Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)".

[UniProt-8] "UniProt, P21549" (jezik: engleski). Pristupljeno 15. 11. 2021.

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