{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T21:07:07Z","timestamp":1791148027751,"version":"4.1.0"},"reference-count":40,"publisher":"Microbiology Society","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,9,1]]},"abstract":"<jats:p><jats:italic>Pseudomonas<\/jats:italic>sp. strain PPD can metabolize phenanthrene as the sole source of carbon and energy via the \u2018phthalic acid\u2019 route. The key enzyme, 1-hydroxy-2-naphthoic acid dioxygenase (1-HNDO, EC 1.13.11.38), was purified to homogeneity using a 3-hydroxy-2-naphthoic acid (3-H2NA)-affinity matrix. The enzyme was a homotetramer with a native molecular mass of 160\u2005kDa and subunit molecular mass of \u223c39\u2005kDa. It required Fe(II) as the cofactor and was specific for 1-hydroxy-2-naphthoic acid (1-H2NA), with<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>13.5\u2005\u03bcM and<jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub>114\u200a\u03bcmol\u2005min<jats:sup>\u22121<\/jats:sup>\u2005mg<jats:sup>\u22121<\/jats:sup>. 1-HNDO failed to show activity with gentisic acid, salicylic acid and other hydroxynaphthoic acids tested. Interestingly, the enzyme showed substrate inhibition with a<jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub>of 116\u2005\u03bcM. 1-HNDO was found to be competitively inhibited by 3-H2NA with a<jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub>of 24\u2005\u03bcM. Based on the pH-dependent spectral changes, the enzyme reaction product was identified as 2-carboxybenzalpyruvic acid. Under anaerobic conditions, the enzyme failed to convert 1-H2NA to 2-carboxybenzalpyruvic acid. Stoichiometric studies showed the incorporation of 1\u2005mol O<jats:sub>2<\/jats:sub>into the substrate to yield 1\u2005mol product. These results suggest that 1-HNDO from<jats:italic>Pseudomonas<\/jats:italic>sp. strain PPD is an extradiol-type ring-cleaving dioxygenase.<\/jats:p>","DOI":"10.1099\/mic.0.030460-0","type":"journal-article","created":{"date-parts":[[2009,8,31]],"date-time":"2009-08-31T22:45:30Z","timestamp":1251758730000},"page":"3083-3091","source":"Crossref","is-referenced-by-count":26,"title":["Biodegradation of phenanthrene by Pseudomonas sp. strain PPD: purification and characterization of 1-hydroxy-2-naphthoic acid dioxygenase"],"prefix":"10.1099","volume":"155","author":[{"given":"Jaigeeth","family":"Deveryshetty","sequence":"first","affiliation":[{"name":"Biotechnology Group, Department of Biosciences and Bioengineering, Indian Institute of Technology \u2013 Bombay, Powai, Mumbai 400\u2005076, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prashant S.","family":"Phale","sequence":"additional","affiliation":[{"name":"Biotechnology Group, Department of Biosciences and Bioengineering, Indian Institute of Technology \u2013 Bombay, Powai, Mumbai 400\u2005076, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0926-6593(66)80147-9","article-title":"Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens","volume":"118","author":"Adachi","year":"1966","journal-title":"Biochim Biophys Acta"},{"key":"R2","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1128\/JB.181.3.757-763.1999","article-title":"Structure of the ring cleavage product of 1-hydroxy-2-naphthoate, an intermediate of the phenanthrene-degradative pathway of Nocardioides sp","volume":"181","author":"Adachi","year":"1999","journal-title":"strain KP7. 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