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Literature summary for 2.7.4.3 extracted from

  • Kleczkowski, L.A.; Randall, D.D.; Zahler, W.L.
    Adenylate kinase from maize leaves: true substrates, inhibition by P1,P5-di(adenosine-5’)pentaphosphate and kinetic mechanism (1990), Z. Naturforsch. C, 45, 607-613.
No PubMed abstract available
Search for more literature for 2.7.4.3

Inhibitors

Inhibitors Comment Organism Structure
P1,P5-diadenosine 5'-pentaphosphate i.e. AP5A or P1,P5-bis(5'-adenosyl)-pentaphosphate, bisubstrate analogue; kinetics Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
 ADP cosubstrate MgADP-, pH 7.8, 25°C Zea mays
0.006
-
 2 ADP cosubstrate ADP, pH 7.8, 25°C Zea mays
0.006
-
 2 ADP ADP in form of MgADP- Zea mays
0.025
-
 ATP cosubstrate AMP, pH 7.8, 25°C Zea mays
0.025
-
 ATP ATP in form of MgATP2- Zea mays
0.069
-
 AMP cosubstrate MgATP, pH 7.8, 25°C Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Zea mays
Mg2+ MgADP- is true substrate Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + ADP Zea mays provides unique buffering role against rapid concentration changes of any component of the adenylate pool ?
-
 ?

Organism

Organism UniProt Comment Textmining
Zea mays
-
 maize
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ADP
-
 Zea mays ATP + AMP
-
 ?
ADP + ADP
-
 Zea mays ATP + AMP
-
 r
ADP + ADP provides unique buffering role against rapid concentration changes of any component of the adenylate pool Zea mays ?
-
 ?
ATP + AMP
-
 Zea mays ADP + ADP
-
 r
ATP + AMP
-
 Zea mays 2 ADP
-
 ?