A5077518647- Porphyrin Metabolism and Disorders
- Folate and B Vitamins Research
- Heme Oxygenase-1 and Carbon Monoxide
- Metabolism and Genetic Disorders
- Biochemical and Molecular Research
- Enzyme Structure and Function
- Cassava research and cyanide
- Metalloenzymes and iron-sulfur proteins
- Polyamine Metabolism and Applications
- Iron Metabolism and Disorders
- Microbial Metabolic Engineering and Bioproduction
- Metal-Catalyzed Oxygenation Mechanisms
- Neonatal Health and Biochemistry
- Enzyme Production and Characterization
- Microbial metabolism and enzyme function
- Diet, Metabolism, and Disease
- Amino Acid Enzymes and Metabolism
- Enzyme Catalysis and Immobilization
- Epigenetics and DNA Methylation
- Yeasts and Rust Fungi Studies
- Reproductive Biology and Fertility
- Biofuel production and bioconversion
- Microbial Metabolism and Applications
- Coordination Chemistry and Organometallics
- Biochemical effects in animals
Okayama University
2012-2024
Bio-Medical Science (South Korea)
2017
Kyoto University
1985-2015
Okayama University of Science
2011
Kyushu University
2004-2009
National Institute of Diabetes and Digestive and Kidney Diseases
2005
Himeji University
2002
Faculty (United Kingdom)
2002
Engineering (Italy)
2002
Adobe Systems (United States)
1988
A series of 16 analogs 5'-deoxy-5 '-adenosylcobalamin (adenosylcobalamin) were examined for their effects on the diol dehydrase system Klebsiella pneumoniae (Aerobacter aerogenes).Four analogs, aru-adenosyl-, aristeromycyl-, 3isoadenosyl-, and nebularylcobalamin, able to function as coenzymes in reaction, coenzyme activity decreasing that order.Like native holoenzyme, complexes enzyme with these four show a cob(II)alamin-like absorption peak or shoulder presence 1,2-propanediol.Analogs...
Klebsiella pneumoniae ( Aerobacter aerogenes ) ATCC 8724 was able to grow anaerobically on 1,2-propanediol and 1,2-ethanediol as carbon energy sources. Whole cells of the bacterium grown or glycerol catalyzed conversion 1,2-diols aldehydes corresponding acids alcohols. Glucose-grown also converted aldehydes, but not 1,2-diols, The presence activities coenzyme B 12 -dependent diol dehydratase, alcohol dehydrogenase, coenzyme-A-dependent aldehyde phosphotransacetylase, acetate kinase...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRole of peripheral side chains vitamin B12 coenzymes in the reaction catalyzed by dioldehydraseTetsuo Toraya, Elizabeth Krodel, Albert S. Mildvan, and Robert H. AbelesCite this: Biochemistry 1979, 18, 3, 417–426Publication Date (Print):February 6, 1979Publication History Published online1 May 2002Published inissue 6 February 1979https://pubs.acs.org/doi/10.1021/bi00570a005https://doi.org/10.1021/bi00570a005research-articleACS PublicationsRequest...
N-terminal truncation of the Escherichia coli ethanolamine ammonia-lyase β-subunit does not affect catalytic properties enzyme (Akita, K., Hieda, N., Baba, Kawaguchi, S., Sakamoto, H., Nakanishi, Y., Yamanishi, M., Mori, and Toraya, T. (2010) J. Biochem. 147, 83–93). The binary complex truncated with cyanocobalamin ternary or adeninylpentylcobalamin substrates were crystallized, their x-ray structures analyzed. exists as a trimer (αβ)2 dimer. active site is in (β/α)8 barrel α-subunit; covers...
Sustained activity of mammalian methionine synthase (MS) requires MS reductase (MSR), but there have been few studies the interactions between these two proteins. In this study, recombinant human (hMS) and MSR (hMSR) were expressed in baculovirus-infected insect cells purified to homogeneity. hMSR maintained hMS at a 1:1 stoichiometric ratio with K(act) value 71 nM. Escherichia coli MS, however, was not activated by hMSR. Moreover, significantly active presence E. flavodoxin reductase, which...
Recombinant glycerol dehydratase of Klebsiella pneumoniae was purified to homogeneity. The subunit composition the enzyme most probably α 2 β γ . When ( R )‐ and S )‐propane‐1,2‐diols were used independently as substrates, rate with )‐enantiomer 2.5 times faster than that )‐isomer. In contrast diol dehydratase, an isofunctional enzyme, affinity for )‐isomer essentially same or only slightly higher K m( ) / = 1.5). crystal structure in complex cyanocobalamin propane‐1,2‐diol determined at 2.1...
The presence of diol dehydratase and glycerol was shown in several bacteria Enterobacteriaceae grown anaerobically on 1,2-propanediol glycerol, respectively. Diol dehydratases were immunologically similar, but distinct from that Propionibacterium freudenreichii.
The catalytic properties of coenzyme B12-dependent glycerol dehydratase and diol were studied in situ with Klebsiella pneumoniae cells permeabilized by toluene treatment, since the enzymes approximate vivo conditions more closely than cell-free extracts or cell homogenates. Both dehydratases underwent rapid "suicidal" inactivation during catalysis, as they do vitro. inactivated situ, however, rapidly continually reactivated adenosine 5'-triphosphate (ATP) Mn2+ presence free...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPropanediol dehydratase system. Role of monovalent cations in binding vitamin B12 coenzyme or its analogs to apoenzymeTetsuo Toraya, Yoshikazu Sugimoto, Yoshikuni Tamao, Shoichi Shimizu, and Saburo FukuiCite this: Biochemistry 1971, 10, 18, 3475–3484Publication Date (Print):August 1, 1971Publication History Published online1 May 2002Published inissue 1 August...
To conduct a concert of CoC bond cleavage and subsequent H-atom abstraction may be the role cob(II)alamin in coenzyme B12 dependent mutases (see picture, Ado=adenosyl). Evidence is presented on basis DFT analysis that these reactions are concerted radicals generated during catalytic process stabilized by presence corrin.
Klebsiella pneumoniae ATCC 25955 (formerly named Aerobacter aerogenes PZH 572, Warsaw), which is known to produce coenzyme-B12-dependent glycerol dehydratase when grown anaerobically in a medium, formed diol 1,2-propanediol-containing medium. Both the and produced by organism catalyzed conversion of glycerol, 1,2-propanediol 1,2-ethanediol corresponding aldehydes underwent concomitant inactivation during catalysis dehydration, as does K. (A. aerogenes) 8724. However, two enzymes were...
Adenosylcobalamin-dependent diol dehydratase of Klebsiella oxytoca undergoes suicide inactivation by glycerol, a physiological substrate. The coenzyme is modified through irreversible cleavage its cobalt-carbon bond, resulting in the enzyme tight binding to active site. Recombinant DdrA and DdrB proteins K. were co-purified homogeneity from cell-free extracts Escherichia coli overexpressing theddrAB genes. They existed as complex,i.e. putative reactivating factor, with an apparent molecular...
Substrate binding triggers catalytic radical formation through the cobalt−carbon bond homolysis in coenzyme B12-dependent enzymes. We have determined crystal structure of substrate-free form Klebsiella oxytoca diol dehydratase·cyanocobalamin complex at 1.85 Å resolution. The contains two units heterotrimer consisting α, β, and γ subunits. As compared with its substrate-bound form, β subunits are tilted by ∼3° cobalamin is also so that pyrrole rings A D significantly lifted up toward...