Prolin

Prolin
Rumus struktur prolin
modél bal-jeung-tongkat	modél ngeusi-rohang
Wasta
	Wasta IUPAC Prolin
	Wasta IUPAC sistematik Asam pirolidin-2-karboksilat
Pananda
Nomer CAS	L: 147-85-3 ; D/L: 609-36-9 ; D: 344-25-2 ;
Modél 3D (JSmol)	L: Gambar interaktif; L Zwitterion: Gambar interaktif;
Rujukan Beilstein	80812
ChEBI	L: CHEBI:17203 ; D/L: CHEBI:26271 ; D: CHEBI:16313 ;
ChEMBL	L: ChEMBL72275 ;
ChemSpider	L: 128566 ; D/L: 594 ; D: 8640 ;
DrugBank	L: DB00172 ;
ECHA InfoCard	100.009.264
Nomer EC	210-189-3
Rujukan Gmelin	26927
KEGG	L: C00148 ;
MeSH	Proline
PubChem CID	L: 145742; D/L: 614; D: 8988;
UNII	L: 9DLQ4CIU6V ; D/L: DCS9E77JPQ ; D: L01Q4LGZ5L ;
CompTox Dashboard (EPA)	L: DTXSID9041104 ;
	InChI InChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1 Key: ONIBWKKTOPOVIA-BYPYZUCNSA-N ; D/L: Key: ONIBWKKTOPOVIA-UHFFFAOYSA-N; D: Key: ONIBWKKTOPOVIA-SCSAIBSYSA-N;
	SMILES L: C1C[C@H](NC1)C(=O)O; L Zwitterion: [O-]C(=O)[C@H](CCC2)[NH2+]2;
Sipat
Rumus kimia	C5H9NO2
Massa molar	115132 g·mol−1
Panampilan	Kristal transparan
Titik lebur	[convert: precision too large] (dékomposa)
Solubilitas	1.5g/100g ethanol 19 degC
log P	-0.06
Kaasaman (pKa)	1.99 (karboksil), 10.96 (amino)
	Iwal disebutkeun séjén, data nu dipidangkeun keur matéri dina kaayaan baku (dina 25 °C, 100 kPa).
	Rujukan kotak info

ALIH Citakan:Disambig info

Artikel ieu lain ngeunaan Proléna.

Prolin (lambang Pro atawa P)^[4] nyaéta asam organik anu jumplukan asam amino protéinogenik (dipaké dina biosintésis protéin), najan teu ngandung gugus amino -NH₂, ngan boga amina sekundér. Nitrogén amina sekundérna dina wangun NH₂⁺ dina kaayaan biologis, anapon gugus karboksil dina wangun −COO⁻. "Ranté gigir" ti karbon α nyambung ka nitrogén ngabentuk buleudan pirolidin, diklasipikasikeun jadi asam amino alipatik. Di manusa teu kaasup ésénsial, sabab ku awak bisa disintésis tina asam amino non-ésénsial L-glutamat. Ieu asam amino dikode ku sakabéh kodon anu dimimitian ku CC (CCU, CCC, CCA, jeung CCG).

Baca ogé

Rujukan

↑ Pubchem. "Proline". pubchem.ncbi.nlm.nih.gov. Diarsipkan dari versi asli tanggal 16 January 2014. Diakses tanggal 8 May 2018.
↑ H.-D. Belitz; W. Grosch; P. Schieberle (2009-01-15). Food Chemistry. p. 15. ISBN 978-3-540-69933-0. Diarsipkan dari versi asli tanggal 2016-05-15.
↑ Nelson, D.L., Cox, M.M., Principles of Biochemistry. NY: W.H. Freeman and Company.
↑ "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Diarsipkan dari versi asli tanggal 9 October 2008. Diakses tanggal 5 March 2018. Archived 9 Oktober 2008 di Wayback Machine

Bacaan salajengna

Balbach, J.; Schmid, F. X. (2000), "Proline isomerization and its catalysis in protein folding", di Pain, R. H., Mechanisms of Protein Folding (2nd ed.), Oxford University Press, pp. 212–49, ISBN 978-0-19-963788-1 .
For a thorough scientific overview of disorders of proline and hydroxyproline metabolism, one can consult chapter 81 of OMMBID Charles Scriver, Beaudet, A.L., Valle, D., Sly, W.S., Vogelstein, B., Childs, B., Kinzler, K.W. (Accessed 2007). The Online Metabolic and Molecular Bases of Inherited Disease. New York: McGraw-Hill. - Summaries of 255 chapters, full text through many universities. There is also the OMMBID blog.

Tutumbu kaluar

Citakan:Modulator reséptor glutamat ionotropik Citakan:Modulator reséptor glisin

[1] Pubchem. "Proline". pubchem.ncbi.nlm.nih.gov. Diarsipkan dari versi asli tanggal 16 January 2014. Diakses tanggal 8 May 2018.

[2] H.-D. Belitz; W. Grosch; P. Schieberle (2009-01-15). Food Chemistry. p. 15. ISBN 978-3-540-69933-0. Diarsipkan dari versi asli tanggal 2016-05-15.

[3] Nelson, D.L., Cox, M.M., Principles of Biochemistry. NY: W.H. Freeman and Company.

[4] "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Diarsipkan dari versi asli tanggal 9 October 2008. Diakses tanggal 5 March 2018. Archived 9 Oktober 2008 di Wayback Machine

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