Katepsin B

Katepsin B
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	3PBH, 1CSB, 1GMY, 1HUC, 1PBH, 2IPP, 2PBH, 3AI8, 3CBJ, 3CBK, 3K9M
Identifikatori
Aliasi	CTSB
Vanjski ID-jevi	OMIM: 116810 MGI: 88561 HomoloGene: 37550 GeneCards: CTSB
Lokacija gena (čovjek)
Hrom.	Hromosom 8 (čovjek)
Kraj	11,869,448 bp
Lokacija gena (miš)
Hrom.	Hromosom 14 (miš)
Kraj	63,383,372 bp
Obrazac RNK ekspresije
	; ; ; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• cysteine-type peptidase activity; • collagen binding; • GO:0070122 peptidase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • cysteine-type endopeptidase activity; • hydrolase activity; • proteoglycan binding; • serine-type endopeptidase activity; • endopeptidase activity;
Ćelijska komponenta	• intracellular membrane-bounded organelle; • Melanosom; • intracellular anatomical structure; • extracellular region; • endolysosome lumen; • Jedarce; • mitohondrija; • Lizozom; • Egzosom; • perinuklearno područje citoplazme; • Vanćelijsko; • ficolin-1-rich granule lumen; • collagen-containing extracellular matrix;
Biološki proces	• regulation of apoptotic process; • epithelial cell differentiation; • Proteoliza; • toll-like receptor signaling pathway; • decidualization; • cellular response to thyroid hormone stimulus; • collagen catabolic process; • viral entry into host cell; • GO:0048552 regulation of catalytic activity; • proteolysis involved in cellular protein catabolic process; • neutrophil degranulation;
	Izvori:Amigo / QuickGO
Ortolozi
	1508
	13030
	ENSG00000164733; ENSG00000285132
	ENSMUSG00000021939
	P07858
	P10605
NM_001908; NM_147780; NM_147781; NM_147782; NM_147783;
	NM_001317237
	NM_007798
NP_001304166; NP_001899; NP_680090; NP_680091; NP_680092;
	NP_680093
	NP_031824
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Katepsin B (EC 3.4.22.1 – katepsin B1 ili katepsin II – je enzim iz superfamilije peptidaza, familija papaina.^[5]^[6]^[7]^[8]^[9]^[10]^[11]^[12] katalizira slijedeću hemijsku reakciju:

Hidroliza proteina široke specifičnosti peptidnih veza. Prvenstveno razlaže -Arg- -Arg- veze u malim molekulama supstrata, po čeme se razlikuje od katepsina L.

Reference

^ ^a ^b ^c ENSG00000285132 GRCh38: Ensembl release 89: ENSG00000164733, ENSG00000285132 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021939 - 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.
^ Cornish-Bowden A. (2004): Fundamentals of enzyme kinetics, 3rd Ed. Portland Press. ISBN 9781855781580; ISBN 1855781581.
^ Međedović S., Maslić E., Hadžiselimović R. (2000): Biologija 2. Svjetlost, Sarajevo, ISBN 9958-10-222-6.
^ Bajrović K, Jevrić-Čaušević A., Hadžiselimović R., Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.
^ Bond, J.S. and Barrett, A.J. (1980). "Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B. A further example of peptidyldipeptidase activity of this proteinase". Biochem. J. 189: 17–25. PMID 7458901.CS1 održavanje: više imena: authors list (link)
^ Barrett, A.J. , Kirschke, H. (1981). "Cathepsin B, cathepsin H and cathepsin L". Methods Enzymol. 80: 535–561. PMID 7043200.CS1 održavanje: više imena: authors list (link)
^ Polgár, L. and Csoma, C. (1987). "Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B". J. Biol. Chem. 262: 14448–14453. PMID 3312190.CS1 održavanje: više imena: authors list (link)
^ Barrett, A.J., Buttle, D.J. and Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256–260.CS1 održavanje: više imena: authors list (link)
^ Kirschke, H., Wikstrom, P. and Shaw, E. (1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Lett. 228: 128–130. PMID 3342870.CS1 održavanje: više imena: authors list (link)

Vanjski linkovi

Cathepsin B na US National Library of Medicine Medical Subject Headings (MeSH)

Logo Commonsa

Cathepsin B na Wikimedia Commonsu.

[refGRCh38Ensembl-1] ENSG00000285132 GRCh38: Ensembl release 89: ENSG00000164733, ENSG00000285132 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021939 - 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.

[5] Cornish-Bowden A. (2004): Fundamentals of enzyme kinetics, 3rd Ed. Portland Press. ISBN 9781855781580; ISBN 1855781581.

[6] Međedović S., Maslić E., Hadžiselimović R. (2000): Biologija 2. Svjetlost, Sarajevo, ISBN 9958-10-222-6.

[7] Bajrović K, Jevrić-Čaušević A., Hadžiselimović R., Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.

[8] Bond, J.S. and Barrett, A.J. (1980). "Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B. A further example of peptidyldipeptidase activity of this proteinase". Biochem. J. 189: 17–25. PMID 7458901.CS1 održavanje: više imena: authors list (link)

[9] Barrett, A.J. , Kirschke, H. (1981). "Cathepsin B, cathepsin H and cathepsin L". Methods Enzymol. 80: 535–561. PMID 7043200.CS1 održavanje: više imena: authors list (link)

[10] Polgár, L. and Csoma, C. (1987). "Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B". J. Biol. Chem. 262: 14448–14453. PMID 3312190.CS1 održavanje: više imena: authors list (link)

[11] Barrett, A.J., Buttle, D.J. and Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256–260.CS1 održavanje: više imena: authors list (link)

[12] Kirschke, H., Wikstrom, P. and Shaw, E. (1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Lett. 228: 128–130. PMID 3342870.CS1 održavanje: više imena: authors list (link)

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