Literature summary for 3.5.4.6 extracted from

Mangani, S.; Benvenuti, M.; Moir, A.J.; Ranieri-Raggi, M.; Martini, D.; Sabbatini, A.R.; Raggi, A.
Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site (2007), Biochim. Biophys. Acta, 1774, 312-322.

Search for more literature for 3.5.4.6

General Stability

General Stability	Organism
an apparent 10000 Da reduction in molecular mass of the native 85000 Da enzyme subunit with its conversion to a 75000 Da core is observed on storage of AMPD	Oryctolagus cuniculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	contains a dinuclear zinc site	Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
70000	-	2 * 85000 (catalytic subunits) + 2 * 70000 (histidine-proline-rich-glycoprotein subunits)	Oryctolagus cuniculus
85000	-	2 * 85000 (catalytic subunits) + 2 * 70000 (histidine-proline-rich-glycoprotein subunits)	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
AMP + H2O	-	Oryctolagus cuniculus	IMP + NH3	-	?

Subunits

Subunits	Comment	Organism
tetramer	2 * 85000 (catalytic subunits) + 2 * 70000 (histidine-proline-rich-glycoprotein subunits)	Oryctolagus cuniculus

Synonyms

Synonyms	Comment	Organism
AmpD	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)