A novel meta-cleavage product hydrolase from Flavobacterium sp. ATCC27551

No Thumbnail Available
Khajamohiddin, Syed
Babu, Pakala Suresh
Chakka, Deviprasanna
Merrick, Mike
Bhaduri, Anirban
Sowdhamini, Ramanathan
Siddavattam, Dayananda
Journal Title
Journal ISSN
Volume Title
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 α/β 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. © 2006 Elsevier Inc. All rights reserved.
α/β Hydrolase, Flavobacterium sp. ATCC27551, Hydrolase, meta-Fission product, meta-Pathway
Biochemical and Biophysical Research Communications. v.351(3)