Document Detail


Cloning of a Sphingomonas paucimobilis SYK-6 gene encoding a novel oxygenase that cleaves lignin-related biphenyl and characterization of the enzyme.
MedLine Citation:
PMID:  9647824     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sphingomonas paucimobilis SYK-6 transforms 2,2'-dihydroxy-3,3'-dimethoxy-5,5'-dicarboxybiphenyl (DDVA), a lignin-related biphenyl compound, to 5-carboxyvanillic acid via 2,2',3-trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl (OH-DDVA) as an intermediate (15). The ring fission of OH-DDVA is an essential step in the DDVA degradative pathway. A 15-kb EcoRI fragment isolated from the cosmid library complemented the growth deficiency of a mutant on OH-DDVA. Subcloning and deletion analysis showed that a 1.4-kb DNA fragment included the gene responsible for the ring fission of OH-DDVA. An open reading frame encoding 334 amino acids was identified and designated ligZ. The deduced amino acid sequence of LigZ had 18 to 21% identity with the class III extradiol dioxygenase family, including the beta subunit (LigB) of protocatechuate 4,5-dioxygenase of SYK-6 (Y. Noda, S. Nishikawa, K.-I. Shiozuka, H. Kadokura, H. Nakajima, K. Yano, Y. Katayama, N. Morohoshi, T. Haraguchi, and M. Yamasaki, J. Bacteriol. 172:2704-2709, 1990), catechol 2,3-dioxygenase I (MpcI) of Alcaligenes eutrophus JMP222 (M. Kabisch and P. Fortnagel, Nucleic Acids Res. 18:3405-3406, 1990), the catalytic subunit of the meta-cleavage enzyme (CarBb) for 2'-aminobiphenyl-2,3-diol from Pseudomonas sp. strain CA10 (S. I. Sato, N. Ouchiyama, T. Kimura, H. Nojiri, H. Yamane, and T. Omori, J. Bacteriol. 179:4841-4849, 1997), and 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) of Escherichia coli (E. L. Spence, M. Kawamukai, J. Sanvoisin, H. Braven, and T. D. H. Bugg, J. Bacteriol. 178:5249-5256, 1996). The ring fission product formed from OH-DDVA by LigZ developed a yellow color with an absorption maximum at 455 nm, suggesting meta cleavage. Thus, LigZ was concluded to be a ring cleavage extradiol dioxygenase. LigZ activity was detected only for OH-DDVA and 2,2',3,3'-tetrahydroxy-5,5'-dicarboxybiphenyl and was dependent on the ferrous ion.
Authors:
X Peng; T Egashira; K Hanashiro; E Masai; S Nishikawa; Y Katayama; K Kimbara; M Fukuda
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Applied and environmental microbiology     Volume:  64     ISSN:  0099-2240     ISO Abbreviation:  Appl. Environ. Microbiol.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-08-11     Completed Date:  1998-08-11     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7605801     Medline TA:  Appl Environ Microbiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2520-7     Citation Subset:  IM    
Affiliation:
Department of Bioengineering, Nagaoka University of Technology, Niigata, Japan.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AB007823;  AB018415
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins*
Base Sequence
Biphenyl Compounds / metabolism*
Escherichia coli / genetics
Lignin / metabolism
Molecular Sequence Data
Oxygenases / genetics*
Phylogeny
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Transformation, Bacterial
Zymomonas / enzymology*,  genetics*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Biphenyl Compounds; 9005-53-2/Lignin; 92-52-4/diphenyl; EC 1.13.-/2,2',3-trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl oxygenase; EC 1.13.-/Oxygenases
Comments/Corrections

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