Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli.

scientific article published on 20 September 2001

Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M107408200
P698PubMed publication ID11567027
P5875ResearchGate publication ID11781148

P50authorMiguel A BallicoraQ59683152
P2093author name stringPreiss J
Frueauf JB
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Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzymeQ38340249
Bacterial glycogen synthesis and its regulationQ40078796
Pyrophosphorylases in Solanum tuberosum: III. PURIFICATION, PHYSICAL, AND CATALYTIC PROPERTIES OF ADPGLUCOSE PYROPHOSPHORYLASE IN POTATOES.Q46098595
Subunit Structure of Spinach Leaf ADPglucose PyrophosphorylaseQ47927627
ADPglucose Pyrophosphorylase Is Encoded by Different mRNA Transcripts in Leaf and Endosperm of CerealsQ47929506
Adenosine 5'-diphosphate-glucose pyrophosphorylase from potato tuber. Significance of the N terminus of the small subunit for catalytic properties and heat stability.Q48071209
Cloning, expression, and nucleotide sequence of glgC gene from an allosteric mutant of Escherichia coli B.Q48168239
Activator-inhibitor interactions in the adenosine diphosphate glucose pyrophosphorylase of Escherichia coli B.Q53714872
Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs.Q54784818
P433issue49
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)46319-46325
P577publication date2001-09-20
P1433published inJournal of Biological ChemistryQ867727
P1476titleAspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli
P478volume276

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cites work (P2860)
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