Literature summary for 2.7.7.42 extracted from

Clancy, P.; Xu, Y.; van Heeswijk, W.C.; Vasudevan, S.G.; Ollis, D.L.
The domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain (2007), FEBS J., 274, 2865-2877.

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Activating Compound

Activating Compound	Comment	Organism	Structure
Gln	C-terminal truncation constructs are dependent on Gln for full adenylylation activity	Escherichia coli
Gln	wild-tpye AT needs both signal transduction protein PII and Gln to stimulate full adenylylation activity	Escherichia coli
signal transduction protein PII	wild-tpye AT needs both signal transduction protein PII and Gln to stimulate full adenylylation activity	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
cloned in Escherichia coli DH5alpha, TG1 and JM109	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	all C-terminal truncation constructs are dependent on Gln for full adenylylation activity	Escherichia coli
additional information	mAbs to AT are used to demonstrate that signal transduction protein PII and signal transduction protein PII-UMP probably bind in the central regulatory domain between residues 466 and 507 to stimulate the adenylylation and deadenylylation reactions, respectively	Escherichia coli
additional information	solubility and enzymatic analysis of several deletion constructs of AT show that AT has three domains: the two activity domains and a central, probably regulatory, domain connected by interdomain Q-linkers (N-Q1-R-Q2-C), the various constructs which have the opposing domain removed, all retain their activity in the absence of their nitrogen status indicator signal transduction protein PII or signal transduction protein PII-UMP	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
adenylyl-[glutamine synthase] + phosphate	deadenylylation reaction	Escherichia coli	glutamine synthase + ADP	-	r
glutamine synthase + ATP	adenylylation reaction	Escherichia coli	adenylyl-[glutamine synthase] + diphosphate	-	r

Synonyms

Synonyms	Comment	Organism
adenylyltransferase	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)