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

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 16 > >>
download as CSV
download all results as CSV
EC Number Protein Variants Commentary Reference
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13D392A kcat lower than wild-type, Km (meso-2,6-diaminoheptanedioate) and Km (ATP) higher than wild-type, Km (UDP-MurNAc-L-Ala-D-Glu) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by at least partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100% 716815
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13D399A site-directed mutagenesis, inactive mutant 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13D399N site-directed mutagenesis, almost inactive mutant 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13DELTA1-24 N-terminal deletion mutant, kcat comparable to wild-type, Km values comparable to wild-type, mutant shows similar results to the wild-type with all the nucleotides, UDP-MurNAc peptides and amino acids 716815
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13E220A kcat lower than wild-type, Km (ATP) and Km (UDP-MurNAc-L-Ala-D-Glu), Km (meso-2,6-diaminoheptanedioate) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by atleast partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100% 716815
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13F340A site-directed mutagenesis, almost inactive mutant 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13F340Y site-directed mutagenesis, the mutant shows reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13H398A site-directed mutagenesis, the mutant shows reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13H398D site-directed mutagenesis, the mutant shows highly reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme 744440
Show all pathways known for 6.3.2.13Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.13K157A kcat lower than wild-type, Km (meso-2,6-diaminoheptanedioate), Km (UDP-MurNAc-L-Ala-D-Glu) and Km (ATP) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by at least partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100% 716815
Results 1 - 10 of 16 > >>
download as CSV
download all results as CSV