Biology:Protein-glutamine glutaminase
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| protein-glutamine glutaminase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.5.1.44 | ||||||||
| CAS number | 62213-11-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction
- protein L-glutamine + H2O protein L-glutamate + NH3
Thus, the two substrates of this enzyme are protein L-glutamine (a glutaminyl residue on a protein) and H2O, whereas its two products are protein L-glutamate (a glutamyl reside on a protein) and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is protein-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase II, glutaminyl-peptide glutaminase, destabilase, and peptidylglutaminase II.
In food production, this enzyme can increase the solubility and potentially reduce the off-flavor of proteins and peptides by forming negatively-charged glutamyl residues. It does not create free glutamin, hence does not add to the umami flavor.[1]
References
- "Peptidoglutaminase. Enzymes for selective deamidation of gamma-amide of peptide-bound glutamine". Biochemistry 10 (7): 1222–9. 1971. doi:10.1021/bi00783a019. PMID 4928623.
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