Arthrobacter ureafaciens

Hoomaert has studied Diels-Alder reactions of pyridine oquinodimethane analogs generated from functionalized o-bis(chloromethyl)pyridines <96T(52)11889>. The photochemical cycloaddition of 2-alkoxy-3-cyano-4,6-dimethylpyridine with methacrylonitrile gives a bicyclic azetine, 6-alkoxy-3,5-dicyano-2,5,8-trimethyl-7-azabicyclo[4.2.0]octa-2,7-diene, in moderate yield <96CC1349>. Regiospecific hydroxylation of 3-(methylaminomethyl)pyridine to 5-(methylaminomethyl)-2-(17/)-pyridone by Arthrobacter ureafaciens has been reported <96MI173>. 

An example of biooxidation is the conversion of the benzyl ether of kojic acid into the benzyl ether of comenic acid by Arthrobacter ureafaciens in a phosphate buffer at pH 12 in up to 97% yield (equation 235) [1044. ... 

Seven different bacterial sialidases, including six commercially available sialidases from Arthrobacter ureafaciens, Clostridium perfingens. Streptococcus sp. IID, Vibrio cholera. Salmonella typhimurium, and Streptococcus pneumoniae, as well as PmSTl which also possesses sialidase activity (20), were used as model systems to test the application of the sialoside library and the 96-well plate based high-throughput colorimetric screening method. 

Ajisaka et al. examined different sialidase somces and found that Newcastle disease virus (NDV) sialidase afforded predominantly the a-2,3 regioisomers, while Arthrobacter ureafaciens and Clostridium perfringens sialidases, in addition to the Vibrio cholerae sialidase examined by Thiem, favored the a-2,6-linked products [53]. Unfortunately, the reaction yields did not improve for the new enzymes, varying from 0.8% to 3.6% isolated yield. In the case of NDV sialidase, the high selectivity for a-2,3-sialosides stemmed from a large a-2,6/a-2,3 hydrolysis ratio. Hydrolysis of the a-2,6 products was found to be 28 times faster than the a-2,3 isomers. Inter-... 

Enzyme technology etc. is still required to maximize the desired yield rather than loss of potential product as carbon dioxide. A new bacterial neuraminidase (from Arthrobacter ureafaciens) has been isolated which is able to hydrolyse the neuraminosyl bond of the ganglioside Gmi- This is the first report of an enzyme with this activity. 

Neuraminidase isolated from the culture filtrate of Arthrobacter ureafaciens has been characterized in detail with respect to its action on glycolipids. Strong electrolytes had a reversible inhibitory effect on the action of the enzyme on brain gangliosides in accordance with Debye-Hiickel effect of ionic environment on ionic activity, and resulted in an acidic shift and a broadening of the pH optimum. Both ionic and non-ionic detergents markedly enhanced the activity of the thiol-sensitive enzyme on the gangliosides, and caused an acidic shift of the pH optimum. It was suggested that the hydrophobic ceramide moiety increases affinity of the lipid substrate to the enzyme, but inhibits hydrolysis of the substrate, possibly due to its hydrophobic interaction with hydrophobic portions of the enzyme molecule. 

Formed by reversion of fructose in strong acid and during hydrol. of inulin. Also by pyrolysis of inulin and bacterial degradn. of inulin with Arthrobacter ureafaciens. Isol. from Lycoris radiata. Cryst. (EtOFO. 

High neuraminidase activities have been shown to be produced by Arthrobacter ureafaciens, A. oxydans, and A. ausescens. Both colominic acid and N acetylneuraminic acid itself were shown to be effective as carbon sources. Affinity chromatographic purification on colominic acid cross-linked to starch by epichlorohydrin gave a product free from phospholipase C, glycoside hydrolases, and A-acetylneuraminic acid aldolase. 

A neuraminidase purified from the culture filtrate of Arthrobacter ureafaciens has been shown to act upon Gmi ganglioside and the oligosaccharide derived therefrom. Addition of detergents, especially bile salts, resulted in a marked increase in the hydrolysis of the intact ganglioside but not of the free oligosaccharide. The actions of neuraminidases from Clostridium perfringens and Vibrio cholerae in the same circumstances were also investigated. 

Uchida Y, Tsukada Y, Sugimori T (1979) Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem 86 1573-1585... 

The use of sialidases for the preparation of acylneuraminic acids has several advantages over the relatively destructive acid hydrolysis techniques. The hydrolysis is carried out under milder conditions of temperature and pH. Low temperatures (0-4 °C) can be employed and even on prolonged incubation (24-48 h) the destruction of released acylneuraminic acids is usually below 5%. The sialic acids are released into aqueous solution at pH 5-6, where they are stable for the duration of the incubation. The use of sialidases is widespread, and several bacterial preparations are available in partially purified form well suited for the experiments outlined here. The most widely available sialidases are those from Vibrio cholerae, Clostridium perfringens and Arthrobacter ureafaciens, and these have sufficiently high specific activities to be used in preparative work. Details of the properties and specificities of these and other sialidases are given in chapter I and in reviews by Drzeniek (1972, 1973) and Corfield et al. (1981). 

Fig. 5. The effect of naturally occurring N-acyl substitution on sialidase activity. A time curve of Neu5Acyl release from sialyl a(2-3)-lactose by Arthrobacter ureafaciens sialidase (A A, 1 mU) and from sialyl a(2-6)-N-acetylgalactosamine by Clostridium perfringens enzyme (O 3.2 mU). The substrates contain either N-acetyl- (O A) or N-glycolyl- ( , A) sialic acids at 1 mM final concentration.

Clostridium perfringens Vibrio cholerae Arthrobacter ureafaciens Newcastle disease virus Influenza A2 virus Fowl plague virus Rat liver Golgi Human liver lysosomal Human fibroblast... 

M. Saito, K. Sugano and Y. Nagai, Action of Arthrobacter ureafaciens on sialoglycolipid substrates. J. Biol Chem. 1979, 254, 7845-7854. 

Uchida, Y., Taikada, Y., and Sugimori, T, 1979, Enzymic properties of a neuraminidase from Arthrobacter ureafaciens, J. Biochem. 86 1573-1585. 

Vibrio cholerae Clostridium perfringens Clostridium chauvoei Bacteroides fragilis Arthrobacter ureafaciens Salmonella typhimuriumf Actinomyces viscosus ... 

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