Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Amber M. Shirley"'
Autor:
Charles W. Finch, Troy D. Klingaman, Amber M. Shirley, Mark A. Storr, Rick W. Chamblee, Paul M. Vassalotti, Walter Thomas, Gary L. Schmitz, Gary M. Fellows, Duane P. Rathmann, Nicholas T. Fassler
Publikováno v:
Agronomy Journal. 103:1697-1703
Autor:
Clint Chapple, John Ralph, Jessica A. Schoenherr, Michael G. Thompson, Mark C. Hall, Amber M. Shirley, Taksina Sinlapadech, Christopher M. Fraser
Publikováno v:
Plant Physiology. 144:1986-1999
The Arabidopsis (Arabidopsis thaliana) genome encodes 51 proteins annotated as serine carboxypeptidase-like (SCPL) enzymes. Nineteen of these SCPL proteins are highly similar to one another, and represent a clade that appears to be unique to plants.
Autor:
Clint Chapple, Amber M. Shirley
Publikováno v:
Journal of Biological Chemistry. 278:19870-19877
Recently, serine carboxypeptidase-like (SCPL) proteins that catalyze transacylation reactions in plant secondary metabolism have been identified from wild tomato and Arabidopsis. These include sinapoylglucose: choline sinapoyltransferase (SCT), an en
Publikováno v:
The Plant Journal. 28:83-94
Serine carboxypeptidase-like (SCPL) proteins have traditionally been assigned roles in the hydrolytic processing of proteins; however, several SCPL proteins have recently been identified as catalysts in transacylation reactions of plant secondary met
Autor:
Joanne C. Cusumano, Dieter Strack, Knut Meyer, Clint Chapple, Amber M. Shirley, Paul V. Viitanen, Max O. Ruegger, Claus Lehfeldt
Publikováno v:
The Plant Cell. 12:1295-1306
Serine carboxypeptidases contain a conserved catalytic triad of serine, histidine, and aspartic acid active-site residues. These enzymes cleave the peptide bond between the penultimate and C-terminal amino acid residues of their protein or peptide su
Publikováno v:
Proceedings of the National Academy of Sciences. 95:6619-6623
The phenylpropanoid pathway provides precursors for the biosynthesis of soluble secondary metabolites and lignin in plants. Ferulate-5-hydroxylase (F5H) catalyzes an irreversible hydroxylation step in this pathway that diverts ferulic acid away from
Autor:
Knut Meyer, Rochus Franke, Amber M. Shirley, Clint Chapple, Colleen M. McMichael, Joanne C. Cusumano
Publikováno v:
The Plant journal : for cell and molecular biology. 22(3)
Ferulate 5-hydroxylase (F5H) is a cytochrome P450-dependent monooxygenase that catalyses the hydroxylation of ferulic acid, coniferaldehyde and coniferyl alcohol in the pathways leading to sinapic acid and syringyl lignin biosynthesis. Earlier studie
Autor:
Claus Lehfeldt, Amber M. Shirley, Knut Meyer, Max O. Ruegger, Joanne C. Cusumano, Paul V. Viitanen, Dieter Strack, Clint Chapple
Publikováno v:
The Plant Cell. 12:1295