Literature DB >> 4395211

Kinetic studies on the reaction mechanism of p-hydroxybenzoate hydroxylase.

S Nakamura, Y Ogura, K Yano, N Higashi, K Arima.   

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Year:  1970        PMID： 4395211     DOI： 10.1021/bi00818a017

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  3 in total

1.  Steady-state kinetic analysis of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath).

Authors:  J Green; H Dalton
Journal:  Biochem J       Date:  1986-05-15       Impact factor: 3.857

2.  Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.

Authors:  W J van Berkel; M H Eppink; H A Schreuder
Journal:  Protein Sci       Date:  1994-12       Impact factor: 6.725

3.  Microbial metabolism of the pyridine ring. The hydroxylation of 4-hydroxypyridine to pyridine-3,4-diol (3,4-dihydroxypyridine) by 4-hydroxypyridine-3-hydroxylase.

Authors:  G K Watson; C Houghton; R B Cain
Journal:  Biochem J       Date:  1974-05       Impact factor: 3.857
  3 in total

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