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2'-dGTP + IMP + L-aspartate
2'-dGDP + phosphate + adenylosuccinate
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
ddGTP + IMP + L-aspartate
ddGDP + phosphate + adenylosuccinate
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
GTP + IMP + 6-methoxypurine nucleotide
?
-
-
-
-
?
GTP + IMP + Ala-3-nitronate
GDP + phosphate + N6-(L-1-carboxy-2-nitroethyl)AMP
-
-
-
?
GTP + IMP + cysteine sulfinate
?
-
-
-
-
?
GTP + IMP + hydroxylamine
GDP + phosphate + ?
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
GTP + ITP + L-aspartate
?
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
ITP + IMP + L-aspartate
IDP + phosphate + adenylosuccinate
-
-
-
?
UTP + IMP + L-Asp
UDP + phosphate + adenylosuccinate
-
-
-
?
XTP + IMP + L-Asp
XDP + phosphate + adenylosuccinate
-
-
-
?
additional information
?
-
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
61% of the efficiency of IMP as substrate, V/Km
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
-
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
-
-
-
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
-
-
-
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
i.e. allopurinol ribonucleotide
-
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
-
-
-
?
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
-
-
-
-
?
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
-
-
-
?
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
-
-
-
-
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
-
-
-
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
-
-
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
-
-
-
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
8.8% of the efficiency of IMP as substrate , V/Km
-
-
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
-
-
-
?
GTP + IMP + L-Asp
?
-
penultimate step in pathway of AMP biosynthesis
-
-
?
GTP + IMP + L-Asp
?
-
plays an important role in the interconversion of purines
-
-
?
GTP + IMP + L-Asp
?
-
plays an important role in the interconversion of purines
-
-
?
GTP + IMP + L-Asp
?
-
first committed step towards the de novo biosynthesis of AMP
-
-
?
GTP + IMP + L-Asp
?
-
first committed step towards the de novo biosynthesis of AMP
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
r
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first step in the de novo synthesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first committed step in de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzing the first committed step in the biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from L-aspartate and IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the first committed step in de novo biosynthesis of AMP plays a significant role in de novo purine nucleotide biosynthesis, the purine nucleotide cycle, and/or salvage pathway for nucleotides
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
salvage pathway
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
key enzyme for the synthesis of adenosine de novo, first committed step in synythesis of adenosine, located at the branchpoint of AMP and GMP synthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first step in the de novo sythesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
i.e. adenylosuccinate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
i.e. adenylosuccinate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
-
-
ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate
-
?
additional information
?
-
-
vertebrates possess two isozymes, the acidic is similar to the synthetase from bacteria and plants, the basic isozyme participates in the purine nucleotide cycle
-
?
additional information
?
-
-
ATP cannot be used as substrate instead of GTP
-
?
additional information
?
-
-
ATP is no substrate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-Asp
?
-
penultimate step in pathway of AMP biosynthesis
-
-
?
GTP + IMP + L-Asp
?
-
plays an important role in the interconversion of purines
-
-
?
GTP + IMP + L-Asp
?
-
plays an important role in the interconversion of purines
-
-
?
GTP + IMP + L-Asp
?
-
first committed step towards the de novo biosynthesis of AMP
-
-
?
GTP + IMP + L-Asp
?
-
first committed step towards the de novo biosynthesis of AMP
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first step in the de novo synthesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first committed step in de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzing the first committed step in the biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from L-aspartate and IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the first committed step in de novo biosynthesis of AMP plays a significant role in de novo purine nucleotide biosynthesis, the purine nucleotide cycle, and/or salvage pathway for nucleotides
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
salvage pathway
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
key enzyme for the synthesis of adenosine de novo, first committed step in synythesis of adenosine, located at the branchpoint of AMP and GMP synthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first step in the de novo sythesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.34
allopurinol ribonucleotide
0.85
beta-D-arabinosylIMP
-
-
additional information
additional information
-
0.041
2'-dIMP
22°C
0.34
allopurinol ribonucleotide
-
-
0.34
allopurinol ribonucleotide
-
Asp, mutant R143L
0.26
arabinosylIMP
-
-
0.26
arabinosylIMP
-
2'-dIMP
0.03
Asp
-
-
0.03
Asp
-
IMP, wild-type
0.0657
Asp
-
mutant R303L
0.115
Asp
-
GTP, mutant S240A
0.23
Asp
-
Asp, wild-type
0.25
Asp
-
skeletal muscle
0.25 - 0.36
Asp
-
muscle enzyme
0.308
Asp
-
Asp, mutant K16Q
0.33
Asp
-
liver basic type L isozyme
0.35
Asp
-
Asp, wild-type, and mutant Q224M
0.36 - 1.47
Asp
-
acidic liver type L isozym
0.44
Asp
-
GTP, mutant K331R
1.47
Asp
-
liver basic type M isozyme
0.17
aspartate
-
pH 7.7, 25°C, mutant D21A
0.23
aspartate
-
pH 7.7, 25°C, wild-type
0.24
aspartate
-
pH 7.7, 25°C, mutant N38E
0.3
aspartate
-
pH 7.7, 25°C, mutant N38A
0.34
aspartate
-
pH 7.7, 25°C, mutant R419L
0.5
aspartate
-
pH 5.6, 25°C, mutant N38D
0.9
aspartate
-
pH 5.6, 25°C, wild-type
1.4
aspartate
-
pH 7.5, 37°C
1.4
aspartate
-
pH 7.7, 25°C, mutant T42A
2
aspartate
-
pH 7.7, 25°C, mutant H41N
2.6
aspartate
-
pH 7.7, 25°C, mutant N38D
0.004 - 0.38
GTP
-
muscle enzyme
0.0044
GTP
-
pH 7.7, 30°C
0.0048
GTP
-
pH 7.5, 37°C
0.009
GTP
-
pH 6.7, 22°C, AdSS1-Tr
0.0091
GTP
-
isoform AdSS1, pH 7.7, 30°C
0.01
GTP
-
Asp, mutant R305L
0.01
GTP
-
isoform AdSS2, pH 7.7, 30°C
0.011
GTP
-
pH 5.6, 25°C, wild-type
0.012
GTP
-
muscle enzyme
0.012
GTP
-
pH 6.7, 22°C, AdSS1
0.013
GTP
-
pH 6.7, 22°C, AdSS2-Tr
0.015
GTP
-
pH 6.7, 22°C, AdSS2
0.015
GTP
22°C, cosubstrate: 2'-dIMP
0.015 - 0.13
GTP
-
liver acidic type L isozyme
0.0172
GTP
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.02
GTP
-
Asp, liver enzyme
0.02
GTP
-
IMP, liver enzyme
0.0201
GTP
-
mutant R303L
0.0206
GTP
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.021
GTP
pH 7.7, 25°C, mutant V273N
0.021
GTP
22°C, cosubstrate: 2'-dIMP
0.023
GTP
-
GTP, mutant K16Q
0.0248
GTP
wild-type, pH 7.0, 37°C
0.0248
GTP
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0251
GTP
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.026
GTP
-
pH 7.7, 25°C, wild-type
0.026
GTP
pH 7.7, 25°C, wild-type
0.026
GTP
22°C, cosubstrate: IMP
0.0265
GTP
-
mutant R304L
0.027
GTP
wild-type, pH 7.0, 25°C
0.027
GTP
mutant N429V, pH 7.0, 37°C
0.0278
GTP
mutant R155L, pH 7.0, 25°C
0.0306
GTP
-
mutant R305L
0.031
GTP
-
GTP, mutant E14A
0.031
GTP
pH 7.7, 25°C, mutant V273A
0.0347
GTP
mutant T307V, pH 7.0, 37°C
0.035
GTP
-
IMP, mutant G15V
0.035
GTP
-
IMP, mutant R131L
0.035
GTP
-
GTP, mutant R131L
0.0358
GTP
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0386
GTP
mutant R155K, pH 7.0, 25°C
0.041
GTP
-
pH 7.7, 25°C, mutant N38A
0.044
GTP
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.045
GTP
pH 7.7, 25°C, mutant V273T
0.0465
GTP
mutant K62L, pH 7.0, 37°C
0.052
GTP
-
pH 7.7, 25°C, mutant D21A
0.054
GTP
-
pH 7.7, 25°C, mutant N38E
0.054
GTP
pH 7.7, 25°C, mutant T128A
0.056
GTP
pH 7.7, 25°C, mutant T300V
0.057
GTP
pH 7.7, 25°C, mutant T301A, hydroxylamine as substrate
0.06
GTP
-
pH 8.0, 25°C, native enzyme
0.0605
GTP
-
mutant Q224M
0.0689
GTP
-
mutant Q224E
0.074
GTP
pH 7.7, 25°C, mutant V273T, hydroxylamine as substrate
0.081
GTP
-
pH 8.0, 25°C, recombinant enzyme
0.0839
GTP
-
mutant L228A
0.09
GTP
-
liver basic type L isozyme
0.116
GTP
-
pH 5.6, 25°C, mutant N38D
0.12
GTP
-
skeletal muscle
0.13
GTP
-
liver basic type L isozyme
0.13
GTP
-
pH 7.7, 25°C, mutant H41N
0.14
GTP
pH 7.7, 25°C, mutant V273A, hydroxylamine as substrate
0.17
GTP
pH 7.7, 25°C, mutant T300A
0.18
GTP
pH 7.7, 25°C, mutant V273N, hydroxylamine as substrate
0.19
GTP
pH 7.7, 25°C, wild-type, hydroxylamine as substrate
0.25
GTP
-
pH 7.7, 25°C, mutant R419L
0.27
GTP
-
pH 7.7, 25°C, mutant N38D
0.28
GTP
-
pH 7.7, 25°C, mutant T42A
1.7
GTP
pH 7.7, 25°C, mutant T129A
91
hydroxylamine
pH 7.7, 25°C, mutant T301A
110
hydroxylamine
pH 7.7, 25°C, mutant V273N
140
hydroxylamine
pH 7.7, 25°C, mutant V273T
230
hydroxylamine
pH 7.7, 25°C, wild-type
255
hydroxylamine
pH 7.7, 25°C, mutant V273A
0.009
IMP
-
pH 6.7, 22°C, AdSS2-Tr
0.012
IMP
-
pH 6.7, 22°C, AdSS2
0.0152
IMP
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0167
IMP
wild-type, pH 7.0, 37°C
0.0168
IMP
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.017
IMP
pH 7.7, 25°C, mutant V273A
0.019
IMP
pH 7.7, 25°C, mutant T300A
0.0198
IMP
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0205
IMP
wild-type, pH 7.0, 25°C
0.0216
IMP
mutant K62L, pH 7.0, 37°C
0.0228
IMP
-
pH 7.5, 37°C
0.024
IMP
pH 7.7, 25°C, mutant V273N
0.0248
IMP
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0276
IMP
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.028
IMP
pH 7.7, 25°C, wild-type
0.028
IMP
-
pH 7.7, 25°C, wild-type and mutant N38E
0.0285
IMP
mutant T307V, pH 7.0, 37°C
0.0292
IMP
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0296
IMP
-
mutant R304L
0.03 - 0.32
IMP
-
liver acidic type L isozyme
0.0305
IMP
-
mutant R305L
0.033
IMP
pH 7.7, 25°C, mutant T300V
0.0352
IMP
-
mutant R303L
0.043
IMP
-
pH 6.7, 22°C, AdSS1-Tr
0.043
IMP
pH 7.7, 25°C, mutant V273T
0.045
IMP
-
pH 6.7, 22°C, AdSS1
0.047
IMP
-
IMP, mutant K331R
0.048
IMP
-
pH 7.7, 25°C, mutant D21A
0.049
IMP
-
pH 7.7, 25°C, mutant N38A
0.0497
IMP
mutant N429V, pH 7.0, 37°C
0.0505
IMP
-
IMP, mutant Q224E
0.054
IMP
-
XTP, mutant D333Q
0.066
IMP
pH 7.7, 25°C, wild-type, hydroxylamine as substrate
0.07
IMP
-
pH 5.6, 25°C, wild-type
0.077
IMP
pH 7.7, 25°C, mutant V273T, hydroxylamine as substrate
0.0825
IMP
-
mutant S240A
0.113
IMP
pH 7.7, 25°C, mutant V273N, hydroxylamine as substrate
0.123
IMP
-
pH 7.7, 25°C, mutant T42A
0.14
IMP
pH 7.7, 25°C, mutant V273A, hydroxylamine as substrate
0.171
IMP
-
muscle enzyme
0.2
IMP
-
pH 8.0, 25°C, recombinant enzyme
0.2
IMP
-
pH 7.7, 25°C, mutant R419L
0.2 - 0.7
IMP
-
muscle enzyme
0.3
IMP
-
pH 8.0, 25°C, native enzyme
0.31
IMP
pH 7.7, 25°C, mutant T128A
0.32
IMP
-
liver basic type L isozyme
0.32
IMP
-
Asp, mutant Q224E
0.32
IMP
pH 7.7, 25°C, mutant T301A, hydroxylamine as substrate
0.4
IMP
-
pH 7.7, 25°C, mutant H41N
0.557
IMP
mutant R155K, pH 7.0, 25°C
0.69
IMP
-
liver basic isozyme
0.7
IMP
-
skeletal muscle
0.89
IMP
pH 7.7, 25°C, mutant T129A
1.6
IMP
-
pH 7.7, 25°C, mutant N38D
1.73
IMP
-
Asp, mutant K331R
2.554
IMP
mutant R155L, pH 7.0, 25°C
3.8
IMP
-
pH 5.6, 25°C, mutant N38D
1.07
ITP
-
mutant D333Q
0.004
L-Asp
22°C, cosubstrate: 2'-dIMP
0.013
L-Asp
22°C, cosubstrate: 2'-dIMP
0.23
L-Asp
22°C, cosubstrate: dIMP
0.31
L-Asp
wild-type, pH 7.0, 37°C
0.37
L-Asp
wild-type, pH 7.0, 25°C
0.48
L-Asp
mutant R155K, pH 7.0, 25°C
0.49
L-Asp
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.57
L-Asp
mutant N429V, pH 7.0, 37°C
0.78
L-Asp
mutant K62L, pH 7.0, 37°C
1.1
L-Asp
mutant T307V, pH 7.0, 37°C
1.32
L-Asp
mutant R155L, pH 7.0, 25°C
1.4
L-Asp
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.73
L-Asp
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.9
L-Asp
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.9
L-Asp
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
3.3
L-Asp
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.01
L-aspartate
-
-
0.14
L-aspartate
-
pH 7.2, 22°C
0.14
L-aspartate
-
pH 6.7, 22°C, AdSS1
0.15
L-aspartate
-
pH 6.7, 22°C, AdSS1-Tr
0.17
L-aspartate
pH 7.7, 25°C, mutant T128A
0.23
L-aspartate
pH 7.7, 25°C, wild-type
0.24
L-aspartate
pH 7.7, 25°C, mutant T129A
0.82
L-aspartate
pH 7.7, 25°C, mutant T300V
0.95
L-aspartate
-
pH 6.7, 22°C, AdSS2
1
L-aspartate
-
pH 8.0, 25°C, native enzyme
1.03
L-aspartate
-
pH 6.7, 22°C, AdSS2-Tr
1.079
L-aspartate
pH 6.0, 70°C
1.65
L-aspartate
-
pH 8.0, 25°C, recombinant enzyme
3.4
L-aspartate
pH 7.7, 25°C, mutant V273T
6.2
L-aspartate
pH 7.7, 25°C, mutant T300A
7
L-aspartate
pH 7.7, 25°C, mutant V273A
9
L-aspartate
pH 7.7, 25°C, mutant V273N
1.27
UTP
-
mutant D333N
0.0286
XTP
-
mutant D333E
0.0331
XTP
-
mutant D333N
additional information
additional information
-
-
-
additional information
additional information
-
effect of metal ions on Km-values
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D13A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
D21A
-
directed mutagenesis
D231A
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
D333E
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333N
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333Q
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
E14A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
G12V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
G15V
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
G17V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
K16Q
-
site-directed mutagenesis
K331l
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
K331R
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
L18R
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
L228A
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
N38D
-
directed mutagenesis
N38E
-
directed mutagenesis
Q224M
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
Q34E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
R132L
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
R143K
-
site-directed mutagenesis
R147L
-
mutant R147L shows increased Km for IMP and GTP relative to the wild-type enzyme, Km for Asp exhibits a modest decrease
R419L
-
directed mutagenesis
S240A
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
S240E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
T128A
site-directed mutagenesis
T129A
site-directed mutagenesis
T300A
site-directed mutagenesis
T301A
site-directed mutagenesis
T42A
-
directed mutagenesis
V273A
site-directed mutagenesis
V273N
site-directed mutagenesis
V273T
site-directed mutagenesis
C328D
the mutant shows reduced Km and increased turnover number for L-aspartate compared to the wild type protein
C328D/C368D
the mutant shows reduced Km and turnover number for L-aspartate compared to the wild type protein
C328S
the mutant exhibits no change in the aspartate Km value but reduced turnover number compared to the wild type protein
C328S/C368S
the mutant shows a 4fold reduced Km for aspartate and reduced turnover number compared to the wild type protein
C368S
the mutant exhibits a 1.7fold increase in the aspartate Km value compared to the wild type protein
K62L
increase in Km values for IMP, GTP and aspartate, respectively
N429V
increase in Km values for IMP, GTP and aspartate, respectively, along with a 5 fold drop in the kcat value
R155A
residue influences both ligand binding and catalysis
R155A/G146R
unlike dimeric wild-type, mainly monomeric. Inactive
R155K
residue influences both ligand binding and catalysis
R155L
residue influences both ligand binding and catalysis
T307V
increase in Km values for IMP, GTP and aspartate, respectively
additional information
-
the activity of AMPsS in crude dialyzed cell extracts is 2times lower in the guaBDELTACBS mutant compared with the wild type strain
P242N
about 50% of wild-type activity. Mutant partially reduces the flux towards AMP derived from IMP and increases the riboflavin synthesis precursor GTP
P242N
-
about 50% of wild-type activity. Mutant partially reduces the flux towards AMP derived from IMP and increases the riboflavin synthesis precursor GTP
-
H41N
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
H41N
-
site-directed mutagenesis
N38A
-
site-directed mutagenesis
N38A
-
directed mutagenesis
R143L
-
mutant enzyme R143L with no change in catalytic constant or Km for Asp, but significantly impaired nucleotide binding, 60fold increased Km for IMP and 10fold increased Km for GTP
R143L
-
although the mutants R143L and D13A have low or no activity independently, when they are mixed, a significant amount of activity is obtained. These results indicate that the subunits exchange with each other to form heterodimers with a single viable active site
R143L
-
site-directed mutagenesis
R303L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R303L
-
site-directed mutagenesis
R304L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R304L
-
site-directed mutagenesis
R305L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R305L
-
site-directed mutagenesis
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