Cloning, Sequencing, and Expression of the Gene Encoding 4-Hydroxy-4-methyl-2-oxoglutarate Aldolase from Pseudomonas ochraceae NGJ1

Maruyama, Kana; Miwa, M; Tsujii, Nobuyuki; Nagai, Tatsuo; Tomita, Naotaka; Harada, Toshiyuki; Sobajima, Hirobumi; Sugisaki, Hiroyuki

doi:10.1271/bbb.65.2701

Cited by 21 publications

(25 citation statements)

References 36 publications

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“…Sequencing of pCHH12 with OLG1 as primer gave a sequence coincident with that of the 3 0 -truncated proL gene reported previously. 19) A restriction map of the 12-kb DNA region is shown in Fig. 3B.…”

Section: Resultsmentioning

confidence: 99%

“…The unidentified gene proX appears not to be a regulatory gene, since it encodes a hydrophobic protein having no helix-turn-helix motif to interact with DNA. 19) It is interesting that proOa has an AraC-type helix-turn-helix motif. This motif is found in the three-dimensional structure of S. paucimobilis E. coli MV1184 harboring various plasmids was inoculated on a PCA-agar plate and incubated at 30 C for 2 d. 1, no plasmid; 2, pUSE5.8; 3, pMHK4.7; 4, pUSE5.8 and pMHK4.7.…”

Section: Discussionmentioning

confidence: 99%

“…The chromosomal DNA of P. ochraceae NGJ1 was prepared as described previously. 19) Charomid 9-28 and pMW239 were obtained from Nippon Gene (Tokyo, Japan), pUC19 and pKF19k from TaKaRa (Kusatsu, Japan), and pBluescript SK from Stratagene (La Jolla, California, U.S.A.). An oligonucleotide OLG1 (5 0 -TCCTGGG-CCTGGATATGTACAAGATGCGCG-3 0 ) was prepared for the sense sequence of nucleotide nos.…”

Section: Methodsmentioning

confidence: 99%

“…17,18) All these enzymes are co-induced in phthalate-grown Pseudomonas ochraceae, 12,15,16,18) suggesting that the genes for the PCA meta-degradation pathway form an operon, which we call the pro operon. 19) The pro genes are divided and arranged divergently in Sphingomonas (formerly Pseudomonas) paucimobilis SYK6 [20][21][22][23][24][25] and Sphingomonas sp. LB126, 3) and thus the genetic structure of the pro operon is unclear (Fig.…”

mentioning

confidence: 99%

“…In previous work, 19) we cloned an EcoRI 7.5-kb DNA fragment from the chromosomal DNA of P. ochraceae NGJ1 (GenBank accession no. AB050935), and found a promoter-like sequence and five pro genes, including an unidentified gene ( proX), a transporter gene ( proT), a 4-oxalomesaconate hydratase gene (proH), a 4-hydroxy-4-methyl-2-oxoglutarate aldolase gene (proA), and a 3 0 -truncated PDC lactonase gene (proL) on the DNA fragment (Fig.…”

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confidence: 99%

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Cloning and Characterization of the Genes Encoding Enzymes for the ProtocatechuateMeta-degradation Pathway ofPseudomonas ochraceaeNGJ1

Maruyama

Shibayama

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Cloning and Characterization of the Genes Encoding Enzymes for the ProtocatechuateMeta-degradation Pathway ofPseudomonas ochraceaeNGJ1

Maruyama

Shibayama

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Recent Developments in Enzymatic Asymmetric CC Bond Formation

Müller

2012

Adv Synth Catal

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Some of the recent developments in enzymatic asymmetric CC bond formation are described in this review. The close relationship of biocatalysis and biosynthesis is highlighted with a special emphasis on diversity and biogenesis. One focus of this review is the creation of tetrasubstituted carbon stereocenters. Members of the supposedly well‐known aldolase and hydroxynitrile lyase enzyme families possess the ability to catalyze the formation of tertiary alcohols. In the case of aldolases, this can occur through intramolecular cyclization or intermolecular asymmetric CC bond formation. Thiamine diphosphate‐dependent YerE has been identified as a potent catalyst for the acyloin condensation with ketones as acceptor substrates. C1 transformations such as methylation or carboxylation are catalyzed in an asymmetric manner by enzymes from different classes, for example S‐adenosylmethionine‐dependent (radical) enzymes or NADPH‐dependent oxidoreductases. Insights from biosynthetic and mechanistic studies of enzymatic reactions proceeding via radical intermediates give valuable hints towards possible applications in biocatalysis. Still, the oxygen sensitivity of many of these biocatalysts poses a considerable challenge for practical applications.

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Enzymatic Synthesis of Tertiary Alcohols

Müller

2014

ChemBioEng Reviews

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Tertiary alcohols are found as a motif in many pharmaceuticals and natural products. Elucidation of their biosynthesis is thus a good starting point for the identification of enzymes for the synthesis of chiral tertiary alcohols. To date, however, relatively few enzymatic methods for such syntheses have been established in biotechnological processes. Whereas secondary alcohols can be efficiently synthesized via the (asymmetric) reduction of ketones, a generally applicable method for the enzymatic synthesis of tertiary alcohols has been more difficult to identify. Herein, a survey of the biocatalytic methods for the synthesis of (chiral) tertiary alcohols is presented. Advantages and disadvantages of the respective methods are discussed from a synthetic point of view.

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Cloning, Sequencing, and Expression of the Gene Encoding 4-Hydroxy-4-methyl-2-oxoglutarate Aldolase from Pseudomonas ochraceae NGJ1

Cited by 21 publications

References 36 publications

Cloning and Characterization of the Genes Encoding Enzymes for the ProtocatechuateMeta-degradation Pathway ofPseudomonas ochraceaeNGJ1

Cloning and Characterization of the Genes Encoding Enzymes for the ProtocatechuateMeta-degradation Pathway ofPseudomonas ochraceaeNGJ1

Recent Developments in Enzymatic Asymmetric CC Bond Formation

Enzymatic Synthesis of Tertiary Alcohols

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