Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Anandamide ( N-arachidonoylethanolamine) and other bioactive N-acylethanolamines are degraded to their corresponding fatty acids and ethanolamine. This hydrolysis is mostly attributed to catalysis by FAAH (fatty acid amide hydrolase), which exhibits an alkaline pH optimum. In addition, we have identified another amidase which catalyses the same reaction exclusively at acidic pH values [Ueda, Yamanaka and Yamamoto (2001) J. Biol. Chem. 276, 35552-35557]. In attempts to find selective inhibitors of this acid amidase, we screened various derivatives of palmitic acid, 1-hexadecanol, and 1-pentadecylamine with N-palmitoylethanolamine as substrate. Here we show that N-cyclohexanecarbonylpentadecylamine inhibits the acid amidase from rat lung with an IC50 of 4.5 microM, without inhibiting FAAH at concentrations up to 100 microM. The inhibition was reversible and non-competitive. This compound also inhibited the acid amidase in intact alveolar macrophages. With the aid of this inhibitor, it was revealed that rat basophilic leukaemia cells possess the acid amidase as well as FAAH. Thus the inhibitor may be a useful tool to distinguish the acid amidase from FAAH in various tissues and cells and to elucidate the physiological role of the enzyme.
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PMID:N-cyclohexanecarbonylpentadecylamine: a selective inhibitor of the acid amidase hydrolysing N-acylethanolamines, as a tool to distinguish acid amidase from fatty acid amide hydrolase. 1468 78

A novel Streptomyces sp. HJ02 can grow using pyridine as only carbon resource and has strong ability of pyridine degradation. The effect of pH, temperature, concentration of pyridine and sucrose addition on biodegradative capacity of Streptomyces sp. HJ02 was examined. The main metabolism pathways and mechanism of pyridine degradation by HJ02 strain were described. The Streptomyces sp. HJ02 degraded 2000 mg/l of pyridine nearly within 8 days. The glucose added in culture inhibited on activity of both SSD and amidase. These two enzymes can act and retain its catalytic ability over wide ranges of temperature and pH. The SSD had a higher activity in alkalescence condition from pH 7.0 to pH 10.0 and was more stable at elevated temperatures from 25 degrees C to 40 degrees C. This strain exhibited both succinate semialdehyde dehydrogenase (EC 1.2.1.24) (SSD) and amidase in free cell extracts obtained from cells grown exclusively on pyridine or with sucrose added, suggesting that the metabolism of pyridine was ripped between C-2 and C-3, and pyridine was hydrolyzed to succinate semialdehyde and formamide.
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PMID:The characteristics and mechanisms of pyridine biodegradation by Streptomyces sp. 1905 11