the aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA
the aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA
the aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA
the aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD. CmaE catalyzes the reverse reaction, in which the aminoacyl group is transferred from CmaD back to CmaA
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains
CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
the enzyme is involved in the biosynthesis of the toxin coronatine by the bacterium Pseudomonas syringae. The toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms
HOME
login
history
all enzymes
BRENDA home
History
2.3.2.28 L-allo-isoleucyltransferase
more
top
Information
