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Featured researches published by Zilian Zhang.


Journal of Bacteriology | 2010

Identification of Novel Acetyltransferase Activity on the Thermostable Protein ST0452 from Sulfolobus tokodaii Strain 7

Zilian Zhang; Jun-ichi Akutsu; Yutaka Kawarabayasi

A 401-residue-long protein, ST0452, has been identified from a thermophilic archaeon, Sulfolobus tokodaii strain 7, as a glucose-1-phosphate thymidylyltransferase (Glc-1-P TTase) homolog with a 170-residue-long extra C-terminus portion. Functional analyses of the ST0452 protein have confirmed that the protein possessed dual sugar-1-phosphate nucleotidylyltransferase (sugar-1-P NTase) activities. The 24 repeats of a signature motif sequence which has been found in bacterial acetyltransferases, (L/I/V)-(G/A/E/D)-XX-(S/T/A/V)-X, were detected at the C terminus of the ST0452 protein. This observation prompted our group to investigate the acetyltransferase activity of the ST0452 protein. Detection of the release of coenzyme A (CoA) from acetyl-CoA and the production of UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) from glucosamine-1-phosphate (GlcN-1-P) and UTP in the presence of the ST0452 protein revealed that this protein possesses the GlcN-1-P-specific acetyltransferase activity. In addition, analyses of substrate specificity showed that acetyltransferase activity of the ST0452 protein is capable of catalyzing the change of galactosamine-1-phosphate (GalN-1-P) to N-acetyl-d-galactosamine-1-phosphate (GalNAc-1-P) as well as GlcN-1-P and that its sugar-1-P NTase activity is capable of producing UDP-GalNAc from GalNAc-1-P and UTP. This is the first report of a thermostable bifunctional enzyme with GalN-1-P acetyltransferase and GalNAc-1-P uridyltransferase activities. The observation reveals that the bacteria-type UDP-GlcNAc biosynthetic pathway from fructose-6-phospate is utilized in this archaeon and represents a novel biosynthetic pathway for producing UDP-GalNAc from GalN-1-P in this microorganism.


Archive | 2012

The Thermostable Enzyme Genes of the dTDP-L-Rhamnose Synthesis Pathway (rmlBCD) from a Thermophilic Archaeon

Maki Teramoto; Zilian Zhang; Motohiro Shizuma; Takashi Kawasaki; Yutaka Kawarabayasi; Noriyuki Nakamura

L-rhamnose is found widely in bacteria and plants (Giraud & Naismith, 2000). It is a common component of the cell wall and the capsule of many pathogenic bacteria, and has been indicated to play an essential role in many pathogenic bacteria (Giraud & Naismith, 2000). L-rhamnose is also found in the cytoplasmic membrane of archaea (Sprott et al., 1983), while pathogenic archaea have not been identified (Eckburg et al., 2003).


Applied and Environmental Microbiology | 2017

Increasing the Thermostable Sugar-1-Phosphate Nucleotidylyltransferase Activities of the Archaeal ST0452 Protein through Site Saturation Mutagenesis of the 97th Amino Acid Position

Yuki Honda; Qian Zang; Yasuhiro Shimizu; Mohammad Dadashipour; Zilian Zhang; Yutaka Kawarabayasi

ABSTRACT The ST0452 protein is a bifunctional protein exhibiting sugar-1-phosphate nucleotidylyltransferase (sugar-1-P NTase) and amino-sugar-1-phosphate acetyltransferase activities and was isolated from the thermophilic archaeon Sulfolobus tokodaii. Based on the previous observation that five single mutations increased ST0452 sugar-1-P NTase activity, nine double-mutant ST0452 proteins were generated with the intent of obtaining enzymes exhibiting a further increase in catalysis, but all showed less than 15% of the wild-type N-acetyl-d-glucosamine-1-phosphate uridyltransferase (GlcNAc-1-P UTase) activity. The Y97A mutant exhibited the highest activity of the single-mutant proteins, and thus site saturation mutagenesis of the 97th position (Tyr) was conducted. Six mutants showed both increased GlcNAc-1-P UTase and glucose-1-phosphate uridyltransferase activities, eight mutants showed only enhanced GlcNAc-1-P UTase activity, and six exhibited higher GlcNAc-1-P UTase activity than that of the Y97A mutant. Kinetic analyses of three typical mutants indicated that the increase in sugar-1-P NTase activity was mainly due to an increase in the apparent kcat value. We hypothesized that changing the 97th position (Tyr) to a smaller amino acid with similar electronic properties would increase activity, and thus the Tyr at the corresponding 103rd position of the Escherichia coli GlmU (EcGlmU) enzyme was replaced with the same residues. The Y103N mutant EcGlmU showed increased GlcNAc-1-P UTase activity, revealing that the Tyr at the 97th position of the ST0452 protein (103rd position in EcGlmU) plays an important role in catalysis. The present results provide useful information regarding how to improve the activity of natural enzymes and how to generate powerful enzymes for the industrial production of sugar nucleotides. IMPORTANCE It is typically difficult to increase enzymatic activity by introducing substitutions into a natural enzyme. However, it was previously found that the ST0452 protein, a thermostable enzyme from the thermophilic archaeon Sulfolobus tokodaii, exhibited increased activity following single amino acid substitutions of Ala. In this study, ST0452 proteins exhibiting a further increase in activity were created using a site saturation mutagenesis strategy at the 97th position. Kinetic analyses showed that the increased activities of the mutant proteins were principally due to increased apparent kcat values. These mutant proteins might suggest clues regarding the mechanism underlying the reaction process and provide very important information for the design of synthetic improved enzymes, and they can be used as powerful biocatalysts for the production of sugar nucleotide molecules. Moreover, this work generated useful proteins for three-dimensional structural analysis clarifying the processes underlying the regulation and mechanism of enzymatic activity.


Journal of Biological Chemistry | 2005

Identification of an Extremely Thermostable Enzyme with Dual Sugar-1-phosphate Nucleotidylyltransferase Activities from an Acidothermophilic Archaeon, Sulfolobus tokodaii strain 7

Zilian Zhang; Masanari Tsujimura; Jun-ichi Akutsu; Mayumi Sasaki; Hideji Tajima; Yutaka Kawarabayasi


Journal of Biochemistry | 2005

Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.

Jun-ichi Akutsu; Zilian Zhang; Masanari Tsujimura; Mayumi Sasaki; Masafumi Yohda; Yutaka Kawarabayasi


Journal of Biochemistry | 2007

Increasing in Archaeal GlcNAc-1-P Uridyltransferase Activity by Targeted Mutagenesis while Retaining its Extreme Thermostability

Zilian Zhang; Jun-ichi Akutsu; Masanari Tsujimura; Yutaka Kawarabayasi


Extremophiles | 2015

Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein

Zilian Zhang; Yasuhiro Shimizu; Yutaka Kawarabayasi


Extremophiles | 2015

Identification and characterization of a thermostable bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3

Jun-ichi Akutsu; Zilian Zhang; Rihito Morita; Yutaka Kawarabayasi


Journal of Bacteriology | 2018

Identification of a Direct Biosynthetic Pathway for UDP–N-Acetylgalactosamine from Glucosamine-6-Phosphate in Thermophilic Crenarchaeon Sulfolobus tokodaii

Mohammad Dadashipour; Mariko Iwamoto; Mohammad Murad Hossain; Jun-ichi Akutsu; Zilian Zhang; Yutaka Kawarabayasi


Applied and Environmental Microbiology | 2018

Improvement of ST0452 GlcNAc-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering

Yuki Honda; Shogo Nakano; Sohei Ito; Mohammad Dadashipour; Zilian Zhang; Yutaka Kawarabayasi

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Yutaka Kawarabayasi

National Institute of Advanced Industrial Science and Technology

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Jun-ichi Akutsu

Tokyo University of Agriculture and Technology

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Masanari Tsujimura

National Institute of Advanced Industrial Science and Technology

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Hideji Tajima

Tokyo University of Agriculture and Technology

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Masafumi Yohda

Tokyo University of Agriculture and Technology

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Mohammad Murad Hossain

National Institute of Advanced Industrial Science and Technology

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