Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.3.2.49: L-alanine-L-anticapsin ligase

This is an abbreviated version!
For detailed information about L-alanine-L-anticapsin ligase, go to the full flat file.

Word Map on EC 6.3.2.49

Reaction

ATP
+
L-alanine
+
L-anticapsin
=
ADP
+
phosphate
+
bacilysin

Synonyms

alanine-anticapsin ligase, BacD, BL00235, BSU37710, EC 6.3.2.28, L-Ala-L-aniticapsin ligase, L-alanine-L-aniticapsin ligase, L-amino acid alpha-ligase, L-amino acid ligase, L-amino-acid ligase, LAL, LAL BL00235, RSp1486a, TabS, YwfE

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.49 L-alanine-L-anticapsin ligase

Engineering

Engineering on EC 6.3.2.49 - L-alanine-L-anticapsin ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S1845A
no significant difference in kcat value between the wild type and the mutant enzyme. 2fold increase in Km-value for L-alanine
Y332A
-
site-directed mutagenesis, mutation of Trp332 to Ala causes the enzyme to hydrolyze ATP, even in the absence of L-Ala, and the structure of this mutant protein show a cavity in the N-terminal substrate-binding pocket
Y75F
no significant difference in kcat value between the wild type and the mutant enzyme, 2fold increase in KM-value for L-phenylalanine
S1845A
-
no significant difference in kcat value between the wild type and the mutant enzyme. 2fold increase in Km-value for L-alanine
-
Y75F
-
no significant difference in kcat value between the wild type and the mutant enzyme, 2fold increase in KM-value for L-phenylalanine
-
additional information