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Details on Person Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms

Class:IdLiteratureReference:500240
_displayNameNovel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
_timestamp2010-02-01 20:36:07
author[Person:500234] Mahnke-Zizelman, DK
[Person:500233] Tullson, PC
[Person:76581] Sabina, RL
created[InstanceEdit:500236] D'Eustachio, P, 2010-02-01
journalJ Biol Chem
modified[InstanceEdit:500242] D'Eustachio, P, 2010-02-01
pages35118-25
pubMedIdentifier9857047
titleNovel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
volume273
year1998
(literatureReference)[CatalystActivityReference:9644036] AMP deaminase activity of AMPD tetramers [cytosol] Platelet AMP deaminase. Purification and kinetic studies
[Reaction:76590] AMP + H2O => IMP + NH4+ (AMPD) [Homo sapiens]
[Complex:76595] AMPD1 tetramer [cytosol] [Homo sapiens]
[Complex:76601] AMPD3 tetramer [cytosol] [Homo sapiens]
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