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Prolin

Ti Wikipédia Sunda, énsiklopédi bébas

Citakan:Other uses

Artikel ieu lain ngeunaanProléna.
Prolin
Rumus struktur prolin
Rumus struktur prolin
Wasta
Wasta IUPAC
Prolin
Wasta IUPAC sistematik
Asam pirolidin-2-karboksilat[1]
Pananda
Modél 3D (JSmol)
80812
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard100.009.264
Nomer EC210-189-3
26927
KEGG
MeSHProline
UNII
  • InChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1 YaY
    Key: ONIBWKKTOPOVIA-BYPYZUCNSA-N YaY
  • D/L:Key: ONIBWKKTOPOVIA-UHFFFAOYSA-N
  • D:Key: ONIBWKKTOPOVIA-SCSAIBSYSA-N
  • L:C1C[C@H](NC1)C(=O)O
  • LZwitterion:[O-]C(=O)[C@H](CCC2)[NH2+]2
Sipat
C5H9NO2
Massa molar115132 g·mol−1
PanampilanKristal transparan
Titik lebur[convert: precision too large](dékomposa)
Solubilitas1.5g/100g ethanol 19 degC[2]
logP-0.06
Kaasaman (pKa)1.99 (karboksil), 10.96 (amino)[3]
Iwal disebutkeun séjén, data nu dipidangkeun keur matéri dinakaayaan baku (dina 25 °C, 100 kPa).
Rujukan kotak info

Prolin (lambangPro atawaP)[4] nyaéta asam organik anu jumplukanasam amino protéinogenik (dipaké dinabiosintésis protéin), najan teu ngandunggugus amino-NH2, ngan bogaamina sekundér. Nitrogén amina sekundérna dina wangun NH2+ dina kaayaan biologis, anapongugus karboksil dina wangun −COO. "Ranté gigir" tikarbon α nyambung ka nitrogén ngabentuk buleudanpirolidin, diklasipikasikeun jadiasam aminoalipatik. Di manusa teu kaasup ésénsial, sabab ku awak bisa disintésis tina asam amino non-ésénsialL-glutamat. Ieu asam aminodikode ku sakabéhkodon 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.Diarsipkeun ti vérsi aslina tanggal 16 January 2014. Diaksés tanggal8 May 2018.
  2. H.-D. Belitz; W. Grosch; P. Schieberle (2009-01-15).Food Chemistry. hlm. 15.ISBN 978-3-540-69933-0.Diarsipkeun ti vérsi aslina 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. Diarsipkeun tiasli tanggal 9 October 2008. Diaksés tanggal5 March 2018.Archived 9 Oktober 2008 diWayback Machine

Bacaan salajengna

[édit |édit sumber]
  • Balbach, J.; Schmid, F. X. (2000), "Proline isomerization and its catalysis in protein folding", dina Pain, R. H. (éd.),Mechanisms of Protein Folding (Édisi 2nd), Oxford University Press, hlm. 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 OMMBIDCharles 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 theOMMBID blog.

Tutumbu kaluar

[édit |édit sumber]
Jejer umum
Dumasar pasipatan
Alipatik
Aromatik
Polar, nir-muatan
Muatan positip (pKa)
Muatan négatip (pKa)
Kasetil-CoA
lisin
leusin
triptopanalanin
G
G→piruvat
sitrat
glisin
serin
G→glutamat
α-ketoglutarat
histidin
prolin
arginin
other
G→propionil-CoA
suksinil-CoA
valin
isoleusin
métionin
tréonin
propionil-CoA
G→fumarat
pénilalanintirosin
G→oksaloasetat
Lianna
Métabolisme sistéin

Citakan:Modulator reséptor glutamat ionotropikCitakan:Modulator reséptor glisin

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