500371-01-7Relevant articles and documents
Polycyclic pyridine oxime-based compound as well as pharmaceutical composition and application thereof
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, (2021/11/26)
The invention discloses a polycyclic pyridine oxime-based compound and a pharmaceutical composition and application thereof, wherein the polycyclic pyridine oxime-based compound is shown as a formula (I). The compound shows strong inhibition of influenza
Spiro pyridone derivative and application
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, (2020/12/29)
The invention discloses a spiro pyridone derivative which has a structure shown in a general formula I in the specification. Researches show that the spiro pyridinone derivative has a relatively strong inhibition effect on the activity of influenza A virus RNA polymerase, and can be applied to the preparation of influenza A virus RNA polymerase activity inhibition and influenza A resistance medicines. The general formula I is shown in the specification.
Purification and characterization of molybdenum-containing aldehyde dehydrogenase that oxidizes benzyl maltol derivative from Pseudomonas nitroreducens SB32154
Hibi, Makoto,Kozono, Iori,Ogawa, Jun,Takeuchi, Michiki
, p. 2390 - 2400 (2020/08/05)
Maltol derivatives are used in a variety of fields due to their metal-chelating abilities. In the previous study, it was found that cytochrome P450 monooxygenase, P450nov, which has the ability to effectively convert the 2-methyl group in a maltol derivative, transformed 3-benzyloxy-2-methyl-4-pyrone (BMAL) to 2-(hydroxymethyl)-3-(phenylmethoxy)-4H-pyran-4-one (BMAL-OH) and slightly to 3-benzyloxy-4-oxo-4 H-pyran-2-carboxaldehyde (BMAL-CHO). We isolated Pseudomonas nitroreducens SB32154 with the ability to convert BMAL-CHO to BMAL-COOH from soil. The enzyme responsible for aldehyde oxidation, a BMAL-CHO dehydrogenase, was purified from P. nitroreducens SB32154 and characterized. The purified BMAL-CHO dehydrogenase was found to be a xanthine oxidase family enzyme with unique structure of heterodimer composed of 75 and 15 kDa subunits containing a molybdenum cofactor and [Fe-S] clusters, respectively. The enzyme showed broad substrate specificity toward benzaldehyde derivatives. Furthermore, one-pot conversion of BMAL to BMAL-COOH via BMAL-CHO by the combination of the BMAL-CHO dehydrogenase with P450nov was achieved.