- Biochemical Characteristization of Propionyl-Coenzyme A Carboxylase Complex of Streptomyces toxytricini
-
Atanas V. Demirev , Anamika Khanal , Nguyen Phan Kieu Hanh , Kyung Tae Nam , Doo Hyun Nam
-
J. Microbiol. 2011;49(3):407-412. Published online June 30, 2011
-
DOI: https://doi.org/10.1007/s12275-011-1122-1
-
-
732
View
-
0
Download
-
10
Crossref
-
 Abstract
 PDF
-
Acyl-CoA carboxylases (ACC) are involved in important primary or secondary metabolic pathways such as fatty acid and/or polyketides synthesis. In the 6.2 kb fragment of pccB gene locus of Streptomyces toxytricini producing a pancreatic inhibitor lipstatin, 3 distinct subunit genes of presumable propionyl-CoA carboxylase (PCCase) complex, assumed to be one of ACC responsible for the secondary metabolism, were identified along with gene for a biotin protein ligase (Bpl). The subunits of PCCase complex were α subunit (AccA3), β subunit (PccB), and auxiliary ε subunit (PccE). In order to disclose the involvement of the PCCase complex in secondary metabolism, some biochemical characteristics of each subunit as well as their complex were examined. In the test of substrate specificity of the PCCase complex, it was confirmed that this complex showed much higher conversion of propionyl-CoA rather than acetyl-CoA. It implies the enzyme complex could play a main role in the production of methylmalonyl-CoA from propionyl-CoA, which is a precursor of secondary polyketide biosynthesis.
-
Citations
Citations to this article as recorded by  - A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
Shiyu Wu, Xue Yu, Yujie Wu, Xiaomin Niu, Ximing Chen, Tuo Chen, Wei Zhang, Guangxiu Liu, Paul Dyson
Microorganisms.2026; 14(4): 733. CrossRef - TetR and OmpR family regulators in natural product biosynthesis and resistance
Rachit S. Patil, Siddhant Sharma, Aditya V. Bhaskarwar, Souparnika Nambiar, Niharika A. Bhat, Mani Kanta Koppolu, Hussain Bhukya
Proteins: Structure, Function, and Bioinformatics.2025; 93(1): 38. CrossRef - The degradation of marine abundant compatible solute dimethylsulfoniopropionate was controlled by TetR-family transcriptional regulator DdaR in Alcaligenes faecalis
Siqiong Xu, Yongchuang Liu, Yujie Ouyang, Jialiang Li, Gongyi Song, Xiaohui Wang, Pan Yang, Yuehui Tang, Lili Li, Jian He, Jiguo Qiu, Cuiwei Chu, Keshi Ma
International Biodeterioration & Biodegradation.2024; 194: 105879. CrossRef - A Permissive Medium Chain Acyl-CoA Carboxylase Enables the Efficient Biosynthesis of Extender Units for Engineering Polyketide Carbon Scaffolds
Jun Zhang, Mengmeng Zheng, Jiayan Yan, Zixin Deng, Dongqing Zhu, Xudong Qu
ACS Catalysis.2021; 11(19): 12179. CrossRef - Increasing the Ascomycin Yield by Relieving the Inhibition of Acetyl/Propionyl-CoA Carboxylase by the Signal Transduction Protein GlnB
Pan Wang, Xin Wang, Ying Yin, Mingliang He, Wei Tan, Wenting Gao, Jianping Wen
Frontiers in Microbiology.2021;[Epub] CrossRef -
AccR, a TetR Family Transcriptional Repressor, Coordinates Short-Chain Acyl Coenzyme A Homeostasis in
Streptomyces avermitilis
Mengya Lyu, Yaqing Cheng, Xiao Han, Ying Wen, Yuan Song, Jilun Li, Zhi Chen, Andrew J. McBain
Applied and Environmental Microbiology.2020;[Epub] CrossRef - Current trends and future prospects of lipstatin: a lipase inhibitor and pro-drug for obesity
Punit Kumar, Kashyap Kumar Dubey
RSC Advances.2015; 5(106): 86954. CrossRef - Biosynthesis of Phenylnannolone A, a Multidrug Resistance Reversal Agent from the Halotolerant Myxobacterium Nannocystis pusilla B150
Sarah M. Bouhired, Max Crüsemann, Celso Almeida, Tilmann Weber, Jörn Piel, Till F. Schäberle, Gabriele M. König
ChemBioChem.2014; 15(5): 757. CrossRef - The TetR Family of Regulators
Leslie Cuthbertson, Justin R. Nodwell
Microbiology and Molecular Biology Reviews.2013; 77(3): 440. CrossRef - Structure and function of biotin-dependent carboxylases
Liang Tong
Cellular and Molecular Life Sciences.2013; 70(5): 863. CrossRef
- Identification and Characterization of Acetyl-CoA Carboxylase Gene Cluster in Streptomyces toxytricini
-
Atanas V. Demirev , Ji Seon Lee , Bhishma R. Sedai , Ivan G. Ivanov , Doo Hyun Nam
-
J. Microbiol. 2009;47(4):473-478. Published online September 9, 2009
-
DOI: https://doi.org/10.1007/s12275-009-0135-5
-
-
843
View
-
0
Download
-
12
Crossref
-
Abstract
PDF
-
The gene locus for acetyl-CoA carboxylase (ACC) involved in the primary metabolism was identified from the genomic library of Streptomyces toxytricini which produces a lipase inhibitor lipstatin. The 7.4 kb cloned gene was comprised of 5 ORFs including accD1, accA1, hmgL, fadST1, and stsF. In order to confirm the biochemical characteristics of AccA1, the gene was overexpressed in Escherichia coli cells, and the recombinant protein was purified through Ni2+ affinity chromatography. Because most of the expressed AccA1 was biotinylated by host E. coli BirA in the presence of D-biotin, the non-biotinylated apo-AccA1 was purified after gene induction without D-biotin, followed by exclusion of holo-AccA1 using streptavidin beads. The separated apo-AccA1 was post-translationally biotinylated by S. toxytricini biotin apo-protein ligase (BPL) in a time- and enzyme-dependent manner. This result supports that this gene cluster of S. toxytricini encodes the functional ACC enzyme subunits to be biotinylated.
-
Citations
Citations to this article as recorded by - Experimental investigation of multi-strain bacterial concrete: Self-healing efficiency, strength, and sorptivity under varied curing conditions
Ran Bir Singh, Ashish Kumar, Divya Sharma, Surya Kant Sahdeo
Journal of Building Engineering.2026; 120: 115552. CrossRef - Origin of the 3-methylglutaryl moiety in caprazamycin biosynthesis
Daniel Bär, Benjamin Konetschny, Andreas Kulik, Houchao Xu, Davide Paccagnella, Patrick Beller, Nadine Ziemert, Jeroen S. Dickschat, Bertolt Gust
Microbial Cell Factories.2022;[Epub] CrossRef - Biotechnological and industrial applications of Streptomyces metabolites
Khushboo, Punit Kumar, Kashyap K. Dubey, Zeba Usmani, Minaxi Sharma, Vijai Kumar Gupta
Biofuels, Bioproducts and Biorefining.2022; 16(1): 244. CrossRef - Development and Optimization of a High-Throughput Screening Assay for Rapid Evaluation of Lipstatin Production by Streptomyces Strains
Michal Híreš, Nora Rapavá, Martin Šimkovič, Ľudovít Varečka, Dušan Berkeš, Svetlana Kryštofová
Current Microbiology.2018; 75(5): 580. CrossRef - De novo biosynthesis of myricetin, kaempferol and quercetin in Streptomyces albus and Streptomyces coelicolor
Laura Marín, Ignacio Gutiérrez-del-Río, Rodrigo Entrialgo-Cadierno, Claudio J. Villar, Felipe Lombó, Marie-Joelle Virolle
PLOS ONE.2018; 13(11): e0207278. CrossRef - Regulation and structure of the heteromeric acetyl-CoA carboxylase
Matthew J. Salie, Jay J. Thelen
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids.2016; 1861(9): 1207. CrossRef - Current trends and future prospects of lipstatin: a lipase inhibitor and pro-drug for obesity
Punit Kumar, Kashyap Kumar Dubey
RSC Advances.2015; 5(106): 86954. CrossRef - Enhanced production of lipstatin from Streptomyces toxytricini by optimizing fermentation conditions and medium
Tingheng Zhu, Lingfei Wang, Weixia Wang, Zhongce Hu, Meilan Yu, Kun Wang, Zhifeng Cui
The Journal of General and Applied Microbiology.2014; 60(3): 106. CrossRef -
Transcriptional Response to Vancomycin in a Highly Vancomycin-Resistant
Streptomyces coelicolor
Mutant
Fernando Santos-Beneit, Lorena T Fernández-Martínez, Antonio Rodríguez-García, Seomara Martín-Martín, María Ordóñez-Robles, Paula Yagüe, Angel Manteca, Juan F Martín
Future Microbiology.2014; 9(5): 603. CrossRef - Equilibrium binding and kinetic characterization of putative tetracycline repressor family transcription regulator Fad35R from Mycobacterium tuberculosis
Sushma Anand, Vijay Singh, Appu Kumar Singh, Monica Mittal, Manish Datt, Bala Subramani, Sangaralingam Kumaran
The FEBS Journal.2012; 279(17): 3214. CrossRef - Biochemical characteristization of propionyl-coenzyme a carboxylase complex of Streptomyces toxytricini
Atanas V. Demirev, Anamika Khanal, Nguyen Phan Kieu Hanh, Kyung Tae Nam, Doo Hyun Nam
The Journal of Microbiology.2011; 49(3): 407. CrossRef - The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini
Atanas V. Demirev, Anamika Khanal, Bhishma R. Sedai, Si Kyu Lim, Min Kyun Na, Doo Hyun Nam
Applied Microbiology and Biotechnology.2010; 87(3): 1129. CrossRef
- Molecular Cloning of the Phospholipase D Gene from Streptomyces sp. YU100 and Its Expression in Escherichia coli
-
Ji-Seon Lee , Munkhtsetseg Bat-Ochir , Atanas V. Demirev , Doo Hyun Nam
-
J. Microbiol. 2009;47(1):116-122. Published online February 20, 2009
-
DOI: https://doi.org/10.1007/s12275-008-0161-8
-
-
890
View
-
0
Download
-
14
Crossref
-
Abstract
PDF
-
The gene for phospholipase D (PLD) of Streptomyces sp. YU100 was cloned from λ phage library and heterologously expressed in Escherichia coli. Using an amplified gene fragment based on the consensus sequences of streptomycetes PLDs, λ phage library of Streptomyces sp. YU100 chromosomal DNA was screened. The sequencing result of BamHI-digested 3.8 kb fragment in a positive phage clone revealed the presence of an open reading frame of a full sequence of PLD gene encoding a 540-amino acid protein including 33-amino acid signal peptide. The deduced amino acid sequence showed a high homology with other Streptomyces PLDs, having the highly conserved ‘HKD’ motifs. The PLD gene excluding signal peptide sequence was amplified and subcloned into a pET-32b(+) expression vector in E. coli BL21(DE3). The recombinant PLD was purified by nickel affinity chromatography and compared the enzyme activity with wild-type PLD. The results imply that the recombinant PLD produced by E. coli had the nearly same enzyme activity as PLD from Streptomyces sp. YU100.
-
Citations
Citations to this article as recorded by - A New Phospholipase D-Producing Bacillus cereus: Taxonomy, Mutagenesis, Fermentation Optimization and Enzyme Characterization
Ying He, Ao Huang, Yun Liu
Applied Biochemistry and Biotechnology.2025; 197(8): 5042. CrossRef - Characterization of a phospholipase D from Streptomyces cinnamoneum SK43.003 suitable for phosphatidylserine synthesis
Mengli Li, Yanfeng Zhou, Xiaoli Duan, Licheng Zhou, Tao Zhang
Biotechnology and Applied Biochemistry.2022; 69(5): 1917. CrossRef - Construction of a Super-Folder Fluorescent Protein-Guided Secretory Expression System for the Production of Phospholipase D in Bacillus subtilis
Haiyang Zhang, Xuehan Li, Qi Liu, Jianan Sun, Francesco Secundo, Xiangzhao Mao
Journal of Agricultural and Food Chemistry.2021; 69(24): 6842. CrossRef - Acyl Chain Specificity of Marine Streptomyces klenkii PhosPholipase D and Its Application in Enzymatic Preparation of Phosphatidylserine
Rongkang Hu, Ruiguo Cui, Dongming Lan, Fanghua Wang, Yonghua Wang
International Journal of Molecular Sciences.2021; 22(19): 10580. CrossRef - Highly Efficient Extracellular Production of Recombinant Streptomyces PMF Phospholipase D in Escherichia coli
Jing Wang, Sheng Xu, Yang Pang, Xin Wang, Kequan Chen, Pingkai Ouyang
Catalysts.2020; 10(9): 1057. CrossRef - Microbial phospholipase D: Identification, modification and application
Zhenxia Zhang, Ming Chen, Wei Xu, Wenli Zhang, Tao Zhang, Cuie Guang, Wanmeng Mu
Trends in Food Science & Technology.2020; 96: 145. CrossRef - Comparison of the expression of phospholipase D from Streptomyces halstedii in different hosts and its over-expression in Streptomyces lividans
Xinyi Tao, Ming Zhao, Ying Zhang, Min Liu, Qinghai Liu, Wei Wang, Feng-Qing Wang, Dongzhi Wei
FEMS Microbiology Letters.2019;[Epub] CrossRef - Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine
Wen-Bin Zhou, Jin-Song Gong, Hai-Juan Hou, Heng Li, Zhen-Ming Lu, Hong-Yu Xu, Zheng-Hong Xu, Jin-Song Shi
Bioengineered.2018; 9(1): 80. CrossRef - Highly active and stable nanobiocatalyst based on in-situ cross-linking of phospholipase D for the synthesis of phosphatidylserine
Sai-Sai Li, Yan Li, Neng-Bing Long, Feng Jiang, Rui-Feng Zhang
International Journal of Biological Macromolecules.2018; 117: 1188. CrossRef - Efficient phosphatidylserine synthesis by a phospholipase D from Streptomyces sp. SC734 isolated from soil‐contaminated palm oil
Saovanee Choojit, Uwe T. Bornscheuer, Apichat Upaichit, Aran H‐Kittikun
European Journal of Lipid Science and Technology.2016; 118(5): 803. CrossRef - Cardiolipin Synthetase Is Involved in Antagonistic Interaction (Reverse CAMP Phenomenon) of Mycoplasma Species with Staphylococcus aureus Beta-Hemolysis
Jonathan D. Kornspan, Shlomo Rottem, Ran Nir-Paz, K. C. Carroll
Journal of Clinical Microbiology.2014; 52(5): 1622. CrossRef - Phospholipase A and glycerophosphodiesterase activities in the cell membrane of Mycoplasma hyorhinis
Jonathan D. Kornspan, Shlomo Rottem
FEMS Microbiology Letters.2012; 332(1): 34. CrossRef - Phospholipase D: Enzymology, Functionality, and Chemical Modulation
Paige E. Selvy, Robert R. Lavieri, Craig W. Lindsley, H. Alex Brown
Chemical Reviews.2011; 111(10): 6064. CrossRef - Expression and Biochemical Characteristics of a Phospholipase D from Bacillus licheniformis
Han-Chul Kang, Sang-Hong Yoon, Chang-Muk Lee, Bon-Sung Koo
Journal of Applied Biological Chemistry.2011; 54(2): 94. CrossRef
- Cloning and Analysis of a Type II Polyketide Synthase Gene Cluster from Streptomyces toxytricini NRRL 15,443
-
Anna Yoo , Atanas V. Demirev , Ji Seon Lee , Sang Dal Kim , Doo Hyun Nam
-
J. Microbiol. 2006;44(6):649-654.
-
DOI: https://doi.org/2462 [pii]
-
-
Abstract
PDF
-
A standard type II polyketide synthase (PKS) gene cluster was isolated while attempting to clone the biosynthetic gene for lipstatin from Streptomyces toxytricini NRRL 15,443. This result was observed using a Southern blot of a PstI-digested S. toxytricini chromosomal DNA library with a 444 bp amplified probe of a ketosynthase (KS) gene fragment. Four open reading frames [thioesterase (TE), β-ketoacyl systhase (KAS), chain length factor (CLF), and acyl carrier protein (ACP)], were identified through the nucleotide sequence determination and analysis of a 4.5 kb cloned DNA fragment. In order to confirm the involvement of a cloned gene in lipstatin biosynthesis, a gene disruption experiment for the KS gene was performed. However, the resulting gene disruptant did not show any significant difference in lipstatin production when compared to wild-type S. toxytricini. This result suggests that lipstatin may not be synthesized by a type II PKS.
|
MSK
