(S)-hidroksinitrilna lijaza

(S)-hidroksinitrilna lijaza
Identifikatori
EC broj4.1.2.47
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

(S)-hidroksinitrilna lijaza (EC 4.1.2.47, (S)-cijanohidrin produkujuća hidroksinitrilna lijaza, (S)-oksinitrilaza, (S)-HbHNL, (S)-MeHNL, hidroksinitrilna lijaza, oksinitrilaza, HbHNL, MeHNL, (S)-selektivna hidroksinitrilna lijaza, (S)-cijanohidrin karbonil-lijaza (formira cijanid)) je enzim sa sistematskim imenom (S)-cijanohidrin lijaza (formira cijanid).[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) alifatični (S)-hidroksinitril cijanid + alifatični aldehid ili keton
(2) aromatična (S)-hidroksinitril cijanid + aromatični aldehid

Ovaj enzim katalizuje razlaganje hidroksinitrila u cijanid i korespondirajući aldehid ili keton.

Reference

  1. ^ Förster, S., Roos, J., Effenberger, F., Wajant, H. and Sprauer, A. (1996). „The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins”. Angew. Chem. Int. Ed. 35: 437—439. 
  2. ^ Bühler, H., Effenberger, F., Förster, S., Roos, J. and Wajant, H. (2003). „Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta”. Chembiochem. 4: 211—216. PMID 12616635. 
  3. ^ Semba, H., Dobashi, Y. and Matsui, T. (2008). „Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor”. Biosci. Biotechnol. Biochem. 72: 1457—1463. PMID 18540112. 
  4. ^ Avi, M., Wiedner, R.M., Griengl, H. and Schwab, H. (2008). „Improvement of a stereoselective biocatalytic synthesis by substrate and enzyme engineering: 2-hydroxy-(4′-oxocyclohexyl)acetonitrile as the model”. Chemistry. 14: 11415—11422. PMID 19006143. 
  5. ^ von Langermann, J., Guterl, J.K., Pohl, M., Wajant, H. and Kragl, U. (2008). „Hydroxynitrile lyase catalyzed cyanohydrin synthesis at high pH-values”. Bioprocess Biosyst. Eng. 31: 155—161. PMID 18204865. 
  6. ^ Schmidt, A., Gruber, K., Kratky, C. and Lamzin, V.S. (2008). „Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis”. J. Biol. Chem. 283: 21827—21836. PMID 18524775. 
  7. ^ Gartler, G., Kratky, C. and Gruber, K. (2007). „Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis”. J. Biotechnol. 129: 87—97. PMID 17250917. 
  8. ^ Wagner, U.G., Schall, M., Hasslacher, M., Hayn, M., Griengl, H., Schwab, H. and Kratky, C. (1996). „Crystallization and preliminary X-ray diffraction studies of a hydroxynitrile lyase from Hevea brasiliensis”. Acta Crystallogr. D Biol. Crystallogr. 52: 591—593. PMID 15299689. 
  9. ^ Schmidt, M., Herve, S., Klempier, N. and Griengl, H. (1996). „Preparation of optically active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis”. Tetrahedron. 52: 7833—7840. 
  10. ^ Klempier, N. & Griengl, H. (1993). „Aliphatic (S)-cyanohydrins by enzyme catalyzed synthesis”. Tetrahedron Lett. 34: 4769—4772. 

Literatura

Spoljašnje veze