scholarly journals Inactivation of gilGT , Encoding a C‐ Glycosyltransferase, and gilOIII , Encoding a P450 Enzyme, Allows the Details of the Late Biosynthetic Pathway to Gilvocarcin V to be Delineated

ChemBioChem ◽  
2006 ◽  
Vol 7 (7) ◽  
pp. 1070-1077 ◽  
Author(s):  
Tao Liu ◽  
Madan Kumar Kharel ◽  
Carsten Fischer ◽  
Andrew McCormick ◽  
Jürgen Rohr
Keyword(s):  
Biosynthetic Pathway ◽  
P450 Enzyme ◽  
Gilvocarcin V

scholarly journals Oxepinamide F biosynthesis involves enzymatic d-aminoacyl epimerization, 3H-oxepin formation, and hydroxylation induced double bond migration

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Liujuan Zheng ◽  
Haowen Wang ◽  
Aili Fan ◽  
Shu-Ming Li
Keyword(s):  
Cytochrome P450 ◽  
Double Bond ◽  
Biosynthetic Pathway ◽  
Hydroxyl Group ◽  
Cytochrome P450 Enzyme ◽  
Double Bond Migration ◽  
Feeding Experiments ◽  
Aspergillus Ustus ◽  
P450 Enzyme ◽  
Derivatives Of

Abstract Oxepinamides are derivatives of anthranilyl-containing tripeptides and share an oxepin ring and a fused pyrimidinone moiety. To the best of our knowledge, no studies have been reported on the elucidation of an oxepinamide biosynthetic pathway and conversion of a quinazolinone to a pyrimidinone-fused 1H-oxepin framework by a cytochrome P450 enzyme in fungal natural product biosynthesis. Here we report the isolation of oxepinamide F from Aspergillus ustus and identification of its biosynthetic pathway by gene deletion, heterologous expression, feeding experiments, and enzyme assays. The nonribosomal peptide synthase (NRPS) OpaA assembles the quinazolinone core with d-Phe incorporation. The cytochrome P450 enzyme OpaB catalyzes alone the oxepin ring formation. The flavoenzyme OpaC installs subsequently one hydroxyl group at the oxepin ring, accompanied by double bond migration. The epimerase OpaE changes the d-Phe residue back to l-form, which is essential for the final methylation by OpaF.

Refactoring the Concise Biosynthetic Pathway of Cyanogramide Unveils Spirooxindole Formation Catalyzed by a P450 Enzyme

2020 ◽  
Vol 59 (33) ◽  
pp. 14065-14069
Author(s):  
Yiguang Zhu ◽  
Qingbo Zhang ◽  
Chunyan Fang ◽  
Yingli Zhang ◽  
Liang Ma ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
P450 Enzyme

Refactoring the Concise Biosynthetic Pathway of Cyanogramide Unveils Spirooxindole Formation Catalyzed by a P450 Enzyme

2020 ◽  
Vol 132 (33) ◽  
pp. 14169-14173
Author(s):  
Yiguang Zhu ◽  
Qingbo Zhang ◽  
Chunyan Fang ◽  
Yingli Zhang ◽  
Liang Ma ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
P450 Enzyme

New insights into heparan sulphate biosynthesis from the study of mutant mice

2002 ◽  
Vol 69 ◽  
pp. 47-57 ◽  
Author(s):  
Catherine L. R. Merry ◽  
John T. Gallagher
Keyword(s):  
Growth Factors ◽  
Biosynthetic Pathway ◽  
Heparan Sulphate ◽  
Mutant Mice ◽  
Gene Products ◽  
Multiple Gene ◽  
Adhesion Proteins ◽  
Ligand Interactions

Heparan sulphate (HS) is an essential co-receptor for a number of growth factors, morphogens and adhesion proteins. The biosynthetic modifications involved in the generation of a mature HS chain may determine the strength and outcome of HS–ligand interactions. These modifications are catalysed by a complex family of enzymes, some of which occur as multiple gene products. Various mutant mice have now been generated, which lack the function of isolated components of the HS biosynthetic pathway. In this discussion, we outline the key findings of these studies, and use them to put into context our own work concerning the structure of the HS generated by the Hs2st-/- mice.

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