N-feruloylglycine deacylase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.71 | ||||||||
CAS no. | 118731-84-3 | ||||||||
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 N-feruloylglycine deacylase (EC 3.5.1.71) is an enzyme that catalyzes the chemical reaction
- N-feruloylglycine + H2O ferulate + glycine
Thus, the two substrates of this enzyme are N-feruloylglycine and H2O, whereas its two products are ferulate and glycine.
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 N-feruloylglycine amidohydrolase. This enzyme is also called N-feruloylglycine hydrolase.
References
- Martens M, Cottenie-Ruysschaert M, Hanselaer R, De Cooman L, Casteele KV, Van Sumere CF (1988). "N-Feruloylglycine amidohydrolase from barley seeds and isolated barley embryos". Phytochemistry. 27 (8): 2457–2463. doi:10.1016/0031-9422(88)87012-2.
- Martens M, Cottenie-Ruysschaert M, Hanselaer R, De Cooman L, Casteele KV, Van Sumere CF (1988). "Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos". Phytochemistry. 27 (8): 2465–2475. doi:10.1016/0031-9422(88)87013-4.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
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3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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