Cyanophycin synthase (L-aspartate-adding) | |||||||||
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Identifiers | |||||||||
EC no. | 6.3.2.29 | ||||||||
CAS no. | 131554-17-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Cyanophycin synthase (L-aspartate-adding) | |||||||
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Identifiers | |||||||
Organism | |||||||
Symbol | cphA | ||||||
UniProt | P73833 | ||||||
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Cyanophycin synthase (L-aspartate-adding) (EC 6.3.2.29, CphA, CphA1, CphA2, cyanophycin synthetase, multi-L-arginyl-poly-L-aspartate synthase) is an enzyme with systematic name cyanophycin:L-aspartate ligase (ADP-forming). [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction
This enzyme requires Mg2+ 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 ligases.
The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
Cyanophycin, also known as CGP or multi-L-arginyl-poly, is a non-protein, non-ribosomally produced amino acid polymer composed of an aspartic acid backbone and arginine side groups.
In enzymology, an aerobactin synthase (EC 6.3.2.39) is an enzyme that catalyzes the chemical reaction
In enzymology, an arginine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, an aspartate—ammonia ligase (ADP-forming) (EC 6.3.1.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-aspartate ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutathionylspermidine synthase is an enzyme that catalyzes the chemical reaction
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction
In enzymology, a trypanothione synthase (EC 6.3.1.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramate—L-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, an adenylyl-[glutamate---ammonia ligase] hydrolase (EC 3.1.4.15) is an enzyme that catalyzes the chemical reaction
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 basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step process comprising three main stages:
CPHA or CPhA may refer to:
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction
(ADP-ribosyl)hydrolase 1, also termed [Protein ADP-ribosylarginine] hydrolase and protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase (EC 3.2.2.19), is an enzyme that in humans is encoded by the ADPRH gene. This enzyme is a specific mono(ADP-ribosyl)hydrolase that catalyses the removal of an ADP-ribosyl modification from target arginine residues of protein substrates. The chemical reactions can formally be described as follows:
Cyanophycinase (EC 3.4.15.6, cyanophycin degrading enzyme, beta-Asp-Arg hydrolysing enzyme, CGPase, CphB, CphE, cyanophycin granule polypeptidase, extracellular CGPase) is an enzyme. It catalyses the following chemical reaction
Cyanophycin synthase (L-arginine-adding) is an enzyme with systematic name cyanophycin:L-arginine ligase (ADP-forming). This enzyme catalyses the following chemical reaction: