Sistéin

l-Sistéin
	; Rumus rangka L-sistéin
Modél bal jeung stik	Modél ngeusi rohang
Wasta
	Wasta IUPAC Cysteine
	Wasta lian Asam 2-amino-3-sulphidrilpropanoat
Pananda
Nomer CAS	52-90-4 ; 52-89-1 (hidroklorida) ;
Modél 3D (JSmol)	Gambar interaktif; Zwitterion: Gambar interaktif;
Abbreviations	Cys, C
ChEBI	CHEBI:15356 ;
ChEMBL	ChEMBL54943 ;
ChemSpider	574 (Rasemat) ; 5653 (L-form) ;
ECHA InfoCard	100.000.145
Nomer EC	200-158-2
Nomer E	E920 (palapis, ...)
IUPHAR/BPS	4782;
KEGG	D00026 ;
PubChem CID	5862;
UNII	K848JZ4886 ; A9U1687S1S (hydrochloride) ;
CompTox Dashboard (EPA)	DTXSID8022876 ;
	InChI InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6) Key: XUJNEKJLAYXESH-UHFFFAOYSA-N ; InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 Key: XUJNEKJLAYXESH-REOHCLBHBU; InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6) Key: XUJNEKJLAYXESH-UHFFFAOYAC;
	SMILES C([C@@H](C(=O)O)N)S; Zwitterion: C([C@@H](C(=O)[O-])[NH3+])S;
Sipat
Rumus kimia	C3H7NO2S
Massa molar	12115 g·mol−1
Panampilan	tipung atawa kristal bodas
Titik lebur	240 °C (464 °F; 513 K) decomposes
Kelarutan dina cai	soluble
Solubilitas	1.5g/100g étanol 19 degC
Rotasi kiral ([α]D)	+9.4° (H2O, c = 1.3)
	Iwal disebutkeun séjén, data nu dipidangkeun keur matéri dina kaayaan baku (dina 25 °C, 100 kPa).
	verifikasi (naon ieu ?)
	Rujukan kotak info

Artikel ieu lain ngeunaan sitosin, sistin, sitisin, atawa sitidin.

Sistéina atawa sistéin (lambang Cys atawa C;^[3] /ˈsɪstɪiːn/)^[4] nyaéta asam amino protéinogenik semiésénsial^[5] anu rumusna HOOC-CH-(NH₂)-CH₂-SH. Ranté gigir tiol dina sistéin osok kapaké dina réaksi énzimatik salaku nukléopil.

Nalika aya salaku résidu katalitik deprotonasi, kadang simbol Cyz dipaké.^[6]^[7] Wangun deprotonasi umumna bisa maké simbol Cym ogé.^[8] Ieu tiol babari kaoksidasi jadi turunan disulpida sistin, anu boga pancén struktural penting dina protéin. Dina ieu kasus, simbol Cyx kadang dipaké.^[8] Nalika dipaké aditip dahareun, nomer E-na E920.

Sistéin dikode ku kodon UGU jeung UGC.

Sistéin jeung métionin anu ngandung walirang leuwih babari kaoksidasi batan asam amino lianna.^[9]^[10]

Baca ogé

Wikimedia Commons mibanda média séjénna nu patali jeung Cysteine .

Rujukan

↑ Belitz, H.-D; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN 9783540699330.
↑ Citakan:RubberBible62nd.
↑ Citakan:IUPAC-IUB amino acids 1983
↑ "cysteine - Definition of cysteine in English by Oxford Dictionaries". Oxford Dictionaries - English. Diakses tanggal 15 April 2018. Archived 25 Séptémber 2016 di Wayback Machine
↑ "The primary structure of proteins is the amino acid sequence". The Microbial World. University of Wisconsin-Madison Bacteriology Department. Diarsipkan dari versi asli tanggal 25 May 2013. Diakses tanggal 16 September 2012. Archived 25 Méi 2013 di Wayback Machine
↑ "python - How can I programmatically add Hydrogen to a PDB structure using BioPython?". Bioinformatics Stack Exchange. Diakses tanggal 2022-05-12.
↑ "type of docking | RosettaCommons". www.rosettacommons.org. Diakses tanggal 2022-05-12.
↑ ^a ^b "Amber Workshop - Tutorial A1 - Section 1: Do some editing of the PDB file". ambermd.org. Diakses tanggal 2022-06-02. Archived 2022-05-22 di Wayback Machine
↑ Bin, P; Huang, R; Zhou, X (2017). "Oxidation Resistance of the Sulfur Amino Acids: Methionine and Cysteine.". BioMed research international 2017: 9584932. doi:10.1155/2017/9584932. PMC 5763110. PMID 29445748. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5763110.
↑ "Functions and evolution of selenoprotein methionine sulfoxide reductases". Biochimica et Biophysica Acta (BBA) - General Subjects 1790 (11): 1471–1477. 2009. doi:10.1016/j.bbagen.2009.04.014. PMC 3062201. PMID 19406207. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3062201.

Bacaan salajengna

"Strong hydrophobic nature of cysteine residues in proteins". FEBS Lett. 458 (1): 69–71. September 1999. doi:10.1016/S0014-5793(99)01122-9. PMID 10518936.

Tutumbu kaluar

Citakan:E number infobox 920-929 Citakan:Intermédiat métabolisme amino amino

[1] Belitz, H.-D; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN 9783540699330.

[2] Citakan:RubberBible62nd.

[3] Citakan:IUPAC-IUB amino acids 1983

[4] "cysteine - Definition of cysteine in English by Oxford Dictionaries". Oxford Dictionaries - English. Diakses tanggal 15 April 2018. Archived 25 Séptémber 2016 di Wayback Machine

[microbial-5] "The primary structure of proteins is the amino acid sequence". The Microbial World. University of Wisconsin-Madison Bacteriology Department. Diarsipkan dari versi asli tanggal 25 May 2013. Diakses tanggal 16 September 2012. Archived 25 Méi 2013 di Wayback Machine

[6] "python - How can I programmatically add Hydrogen to a PDB structure using BioPython?". Bioinformatics Stack Exchange. Diakses tanggal 2022-05-12.

[7] "type of docking | RosettaCommons". www.rosettacommons.org. Diakses tanggal 2022-05-12.

[:0-8] "Amber Workshop - Tutorial A1 - Section 1: Do some editing of the PDB file". ambermd.org. Diakses tanggal 2022-06-02. Archived 2022-05-22 di Wayback Machine

[9] Bin, P; Huang, R; Zhou, X (2017). "Oxidation Resistance of the Sulfur Amino Acids: Methionine and Cysteine.". BioMed research international 2017: 9584932. doi:10.1155/2017/9584932. PMC 5763110. PMID 29445748. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5763110.

[BCLee-10] "Functions and evolution of selenoprotein methionine sulfoxide reductases". Biochimica et Biophysica Acta (BBA) - General Subjects 1790 (11): 1471–1477. 2009. doi:10.1016/j.bbagen.2009.04.014. PMC 3062201. PMID 19406207. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3062201.

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