Prolin

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Prolin
Rumus struktur prolin
L-proline-skeletal.png
Proline-from-xtal-3D-bs-17-view-B.png
Proline-from-xtal-3D-sf-view-B.png
Wasta
Wasta IUPAC
Prolin
Wasta IUPAC sistematik
Asam pirolidin-2-karboksilat[1]
Pananda
Modél 3D (JSmol)
80812
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.009.264
Nomer EC 210-189-3
26927
KEGG
MeSH Proline
UNII
Sipat
C5H9NO2
Massa molar 115132 g·mol−1
Panampilan Kristal transparan
Titik lebur [convert: precision too large] (dékomposa)
Solubilitas 1.5g/100g ethanol 19 degC[2]
log P -0.06
Kaasaman (pKa) 1.99 (karboksil), 10.96 (amino)[3]
Iwal disebutkeun séjén, data nu dipidangkeun keur matéri dina kaayaan baku (dina 25 °C, 100 kPa).
Rujukan kotak info

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[édit | édit sumber]

Rujukan[édit | édit sumber]

  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. 

Bacaan salajengna[édit | édit sumber]

  • 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[édit | édit sumber]

Citakan:Modulator reséptor glutamat ionotropik Citakan:Modulator reséptor glisin