|Gene:||GDA||Accession Number: G-11616 (MetaCyc)|
Species: Homo sapiens
The native apparent molecular mass was determined by gel filtration chromatography [Gupta85].
Native human liver enzyme has been purified and characterized [Gupta85, Ito90]. Recombinant enzyme has also been expressed in Escherichia coli, purified and characterized. Mn2+ stimulated the activity of the recombinant enzyme approximately 2-fold. Although no Mn2+ was found to be bound to the recombinant enzyme, the monomers contained Zn2+ [Yuan99].
This enzyme is present mainly in human liver, brain and kidney. It has been immunohistochemically localized in the cytoplasm of hepatocytes, small intestine mucosal epithelium and kidney proximal tubules [Kubo06]. Evidence for two isozymes was obtained during purification of the enzyme at the HPLC ion exchange chromatography step [Ito90].
The subunit apparent molecular mass was determined by SDS-PAGE [Gupta85].
|Map Position: [74,764,293 -> 74,867,140]|
Molecular Weight of Polypeptide: 51.003 kD (from nucleotide sequence), 59.0 kD (experimental) [Gupta85 ]
Molecular Weight of Multimer: 120.0 kD (experimental) [Gupta85]
pI: 4.76 [Gupta85]
Unification Links: ArrayExpress:Q9Y2T3 , Entrez-gene:9615 , Mint:MINT-109340 , PhosphoSite:Q9Y2T3 , PhylomeDB:Q9Y2T3 , Pride:Q9Y2T3 , Protein Model Portal:Q9Y2T3 , SMR:Q9Y2T3 , String:9606.ENSP00000351170 , UniProt:Q9Y2T3
Relationship Links: InterPro:IN-FAMILY:IPR006680 , InterPro:IN-FAMILY:IPR014311 , Panther:IN-FAMILY:PTHR11271:SF6 , PDB:Structure:2UZ9 , PDB:Structure:3E0L , PDB:Structure:4AQL , Pfam:IN-FAMILY:PF01979
|Cellular Component:||GO:0005737 - cytoplasm [Kubo06]|
Enzymatic reaction of: ammeline deaminase (guanine deaminase)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is favored in the direction shown.
The purified enzyme was shown to possess an ammeline deaminase activity of 57 nmol per min per mg [Seffernick10].
Enzymatic reaction of: guanine deaminase
Synonyms: guanase, guanine aminase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown. [Yuan99]
In mammals this enzyme reaction of purine catabolism is considered to be physiologically irreversible in the left to right direction. The production of xanthine and ammonia prevent reutilization of the guanine base (in [Yuan99]).
pH(opt): 8.0 [Gupta85]
Kubo06: Kubo K, Honda H, Sannomiya K, Aying Y, Mei W, Mi S, Aoyagi E, Simizu I, Ii K, Ito S (2006). "Histochemical and immunohistochemical investigation of guanase and nedasin in human tissues." J Med Invest 53(3-4);264-70. PMID: 16953063
Yuan99: Yuan G, Bin JC, McKay DJ, Snyder FF (1999). "Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein." J Biol Chem 274(12);8175-80. PMID: 10075721
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