A novel salicylaldehyde dehydrogenase-NahV involved in catabolism of naphthalene from Pseudomonas putida ND6
A novel salicylaldehyde dehydrogenase-NahV involved in catabolism of naphthalene from Pseudomonas putida ND6
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一种新型水杨醛脱氢酶-NahV参与恶臭假单胞菌ND6萘的分解代谢
DOI:
10.1007/s11434-007-0296-8
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发表时间:
2007-07
期刊:
影响因子:
--
通讯作者:
Li, YongJun
中科院分区:
文献类型:
--
作者:
Zhao, HuaBing;Cai, BaoLi;Chen, Wei;Li, YongJun
A novel salicylaldehyde dehydrogenase involved in catabolism of naphthalene from Pseudomonas putida ND6, NahV, has been identified. NahV exhibited lower identity in amino acid sequence with the classic salicylaldehyde dehydrogenase, NahF, from P. putida ND6. This is the first report of an isofunctional enzyme of bacterial salicylaldehyde dehydrogenase. Both enzymes exhibited broad substrate specificities and catalyzed the oxidation of salicylaldehyde, 5-chlorosalicylaldehyde, formaldehyde, m-nitrobenzaldehyde, o-nitrobenzaldehyde, o-methoxybenxaldehyde, glutaraldehyde, caprylic aldehyde, and glyoxal. However, the relative rates at which the substituted analogs are transformed differ considerably. NahV activity could be enhanced by Fe2+, Cu2+ and Zn2+; whereas NahF activity could only be stimulated by Fe2+. NahF is more stable than NahV at elevated temperatures. Dot-blot hybridization analyses showed that nahF-like genes occurred in all naphthalene-degradation bacteria isolated in this study, whereas nahV-like genes were present in only some naphthalene-degrading bacteria.
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影响因子:
3.2
作者:
Sota, M;Yano, H;Tsuda, M
通讯作者:
Tsuda, M
DOI:
--
发表时间:
2001-01
期刊:
--
影响因子:
--
作者:
J. Sambrook;E. Fritsch;T. Maniatis
通讯作者:
J. Sambrook;E. Fritsch;T. Maniatis
影响因子:
4.4
作者:
Jeon, CO;Park, M;Madsen, EL
通讯作者:
Madsen, EL
影响因子:
3.2
作者:
Caroline M. Laemmli;J. Leveau;A. Zehnder;J. R. van der Meer
通讯作者:
Caroline M. Laemmli;J. Leveau;A. Zehnder;J. R. van der Meer
影响因子:
3.5
作者:
Bosch, R;García-Valdés, E;Moore, ERB
通讯作者:
Moore, ERB