Cyanophycin synthase (
L-aspartate-adding) (, ''CphA'', ''CphA1'', ''CphA2'', ''cyanophycin synthetase'', ''multi-L-arginyl-poly-L-aspartate synthase'') is an
enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
with
systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature.
A semisystematic name or semitrivial ...
''cyanophycin:L-aspartate ligase (ADP-forming)''.
This enzyme
catalyses the following
chemical reaction
A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ...
: ATP +
-Asp(4-L-Arg) + L-Asp
ADP +
phosphate
In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid .
The phosphate or orthophosphate ion is derived from phospho ...
+
-Asp(4-L-Arg)-L-Asp
This enzyme requires Mg
2+ for activity. All enzymes known to have this activity also catalyze the addition of arginine, i.e.
cyanophycin synthase (L-arginine-adding) activity. It is structurally similar to
Muramyl ligase
The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The ...
s.
References
External links
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EC 6.3.2