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  • protein
  • Mutations in alpha-synuclein, UCHL1 (a ubiquitin carboxy-terminal hydrolase L1), parkin, DJ1 (a parkin-associated protein involved with oxidative stress), and PINK1 (a putative serine threonine kinase) are known to cause early-onset PD. (genome.jp)
  • acid
  • Vernolic acid (leukotoxins) and Coronaric acids (isoleukotoxins) to their corresponding diols which are highly toxic in animal models and possibly humans (see Vernolic acid#toxicity, Coronaric acid#toxicity, and soluble epoxide hydrolase). (wikipedia.org)
  • enzymology
  • In enzymology, a phosphonoacetaldehyde hydrolase (EC 3.11.1.1) is an enzyme that catalyzes the chemical reaction phosphonoacetaldehyde + H2O ⇌ {\displaystyle \rightleftharpoons } acetaldehyde + phosphate Thus, the two substrates of this enzyme are phosphonoacetaldehyde and H2O, whereas its two products are acetaldehyde and phosphate. (wikipedia.org)
  • In enzymology, a phloretin hydrolase (EC 3.7.1.4) is an enzyme that catalyzes the chemical reaction phloretin + H2O ⇌ {\displaystyle \rightleftharpoons } phloretate + phloroglucinol Thus, the two substrates of this enzyme are phloretin and H2O, whereas its two products are phloretate and phloroglucinol. (wikipedia.org)
  • In enzymology, an acyloxyacyl hydrolase (EC 3.1.1.77) is an enzyme that catalyzes the chemical reaction 3-(acyloxy)acyl group of bacterial lipopolysaccharide (lipid A moiety) ⇌ {\displaystyle \rightleftharpoons } 3-hydroxyacyl group of bacterial lipopolysaccharide + a fatty acid Hence, this enzyme has one substrate, the 3-(acyloxy)acyl groups of bacterial lipopolysaccharides, and two products, [partially deacylated lipopolysaccharide] and fatty acid. (wikipedia.org)
  • In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction allophanate + 3 H2O + H+ ⇌ {\displaystyle \rightleftharpoons } 2 HCO3− + 2 NH4+ Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+. (wikipedia.org)
  • In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction 5-hydroxyisourate + H2O ⇌ {\displaystyle \rightleftharpoons } 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate Thus, the two substrates of this enzyme are 5-hydroxyisourate and H2O, whereas its product is 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate. (wikipedia.org)
  • In enzymology, a chlorogenate hydrolase (EC 3.1.1.42) is an enzyme that catalyzes the chemical reaction chlorogenate + H2O ⇌ {\displaystyle \rightleftharpoons } caffeate + quinate Thus, the two substrates of this enzyme are chlorogenate and H2O, whereas its two products are caffeate and quinate. (wikipedia.org)
  • In enzymology, a Hydroxyacylglutathione hydrolase (EC 3.1.2.6) is an enzyme that catalyzes the chemical reaction (R)-S-lactoylglutathione + water ⇌ {\displaystyle \rightleftharpoons } glutathione + a 2-hydroxy carboxylate Hence, this enzyme has two substrates, (R)-S-lactoylglutathione and water, and two products, glutathione and a 2-hydroxy carboxylate. (wikipedia.org)
  • PMID
  • A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ PMID: 7624375 , PMID: 8535779 ]. (ebi.ac.uk)
  • One of these families is known as the cellulase family K or as the glycosyl hydrolases family 45 [ PMID: 8352747 ]. (ebi.ac.uk)
  • This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor [ PMID: 8083158 ]. (ebi.ac.uk)
  • and are inactivated by bleomycin hydrolase, which hydrolyses the carboxyamide bond of the beta-aminoalanine moiety [ PMID: 4122312 ]. (ebi.ac.uk)
  • Bleomycin hydrolase acts mainly as an aminopeptidase on short peptides, but the rat orthologue has been shown to cleave amyloid beta-peptides, acting as an endopeptidase or a carboxypeptidase, as well as an aminopeptidase [ PMID: 16472072 ]. (ebi.ac.uk)
  • Bleomycin hydrolase is intracellular and exists naturally as a homohexamer, with all the active site in the central cavity of the barrel [ PMID: 7638617 ]. (ebi.ac.uk)
  • This domain is also found in lysophospholipases such as cytosolic phospholipase A2 (which has additional structural features) [ PMID: 10319815 ], and in patatin proteins, which are plant glycoproteins that act as non-specific lipid acyl hydrolases [ PMID: 12779324 ]. (ebi.ac.uk)
  • Fatty-acid amide hydrolase 1 (FAAH) is a mammalian integral membrane enzyme that degrades the fatty acid amide family of endogenous signalling lipids, which includes the endogenous cannabinoid anandamide and the sleep-inducing substance oleamide [ PMID: 15952893 ]. (ebi.ac.uk)
  • catalyzes
  • An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. (ebi.ac.uk)
  • For example, an enzyme that catalyzes the following reaction is a hydrolase: A-B + H2O → A-OH + B-H Systematic names of hydrolases are formed as "substrate hydrolase. (wikipedia.org)
  • esterase
  • This entry represents the SGNH hydrolase-type esterase domain, which has a similar fold to flavoproteins, namely a three-layer alpha/beta/alpha structure, where the beta-sheets are composed of five parallel strands. (ebi.ac.uk)