A novel meta-cleavage product hydrolase from Flavobacterium sp. ATCC27551
| Autor: | Pakala Suresh Babu, Syed Khajamohiddin, Deviprasanna Chakka, Mike Merrick, Anirban Bhaduri, Ramanathan Sowdhamini, Dayananda Siddavattam |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Hydrolases Protein Conformation Molecular Sequence Data Biophysics Flavobacterium Biochemistry Catalysis Hydrolase Gene cluster Catalytic triad Computer Simulation Amino Acid Sequence Homology modeling Molecular Biology Binding Sites biology Structural gene Active site Cell Biology biology.organism_classification Enzyme Activation Models Chemical biology.protein Protein Binding Homotetramer |
| Zdroj: | Biochemical and Biophysical Research Communications. 351:675-681 |
| ISSN: | 0006-291X |
| Popis: | The organophosphate degrading (opd) gene cluster of plasmid pPDL2 of Flavobacterium sp. ATCC27551 contains a novel open-reading frame, orf243. This was predicted to encode an alpha/beta hydrolase distantly related to the meta-fission product (MFP) hydrolases such as XylF, PhnD, and CumD. By homology modeling Orf243 has most of the structural features of MFP hydrolases including the characteristic active site catalytic triad. The purified protein (designated MfhA) is a homotetramer and shows similar affinity for 2-hydroxy-6-oxohepta-2,4-dienoate (HOHD), 2-hydroxymuconic semialdehyde (HMSA), and 2-hydroxy-5-methylmuconic semialdehyde (HMMSA), the meta-fission products of 3-methyl catechol, catechol, and 4-methyl catechol. The unique catalytic properties of MfhA and the presence near its structural gene of cis-elements required for transposition suggest that mfhA has evolved towards encoding a common hydrolase that can act on meta-fission products containing either aldehyde or ketone groups. |
| Databáze: | OpenAIRE |
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