Literature summary for 3.5.4.6 extracted from

Ronca, F.; Raggi, A.
Role of the HPRG component of striated muscle AMP deaminase in the stability and cellular behaviour of the enzyme (2018), Biomolecules, 8, E79 .

Search for more literature for 3.5.4.6

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	metalloenzyme. The metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, it is hypothesized that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament	Oryctolagus cuniculus
Zn2+	metalloenzyme. The metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, it is hypothesized that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament	Rattus norvegicus
Zn2+	metalloenzyme. The metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, it is hypothesized that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament	Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
AMP + H2O	Oryctolagus cuniculus	-	IMP + NH3	-	ir

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	P81073	-	-
Oryctolagus cuniculus	P81072	-	-
Rattus norvegicus	P10759	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	-	Oryctolagus cuniculus	-
skeletal muscle	-	Rattus norvegicus	-
skeletal muscle	-	Gallus gallus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
AMP + H2O	-	Oryctolagus cuniculus	IMP + NH3	-	ir
AMP + H2O	-	Rattus norvegicus	IMP + NH3	-	ir
AMP + H2O	-	Gallus gallus	IMP + NH3	-	ir

Synonyms

Synonyms	Comment	Organism
AMPD1	-	Oryctolagus cuniculus
AMPD1	-	Rattus norvegicus
AMPD1	-	Gallus gallus
muscle AMP deaminase	-	Oryctolagus cuniculus
muscle AMP deaminase	-	Rattus norvegicus
muscle AMP deaminase	-	Gallus gallus

General Information

General Information	Comment	Organism
physiological function	the enzyme appears to play a role in regulation of relative concentrations of intracellular purine nucleotide pools, the stabilization of adenylate energy charge, and the deamination of amino acids via the purine nucleotide cycle	Oryctolagus cuniculus
physiological function	the enzyme appears to play a role in regulation of relative concentrations of intracellular purine nucleotide pools, the stabilization of adenylate energy charge, and the deamination of amino acids via the purine nucleotide cycle	Rattus norvegicus
physiological function	the enzyme appears to play a role in regulation of relative concentrations of intracellular purine nucleotide pools, the stabilization of adenylate energy charge, and the deamination of amino acids via the purine nucleotide cycle	Gallus gallus

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Release 2023.1 (January 2023)