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2.7.7.89: [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

This is an abbreviated version!
For detailed information about [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase, go to the full flat file.

Reaction

[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
+
phosphate
=
[glutamine synthetase]-L-tyrosine
+
ADP

Synonyms

adenylyl(glutamine synthetase) hydrolase, adenylyl-[glutamine-synthetase] hydrolase, EC 3.1.4.15, GlnE, hydrolase adenylyl(glutamine synthetase), [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.89 [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

Crystallization

Crystallization on EC 2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase, to 2.0 A resolution. The domain has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all adenylyltransferase sequences clusters around the active site
crystallization of a soluble N-terminal domain, residues 1-440, to 2.6 A resolution