LIVIVO - Search results -

Search results

Result 1 - 10 of total 13

Search options

Article ; Online: Amides in Nature and Biocatalysis.

Pitzer, Julia / Steiner, Kerstin

2016 Volume 235, Page(s) 32–46

Abstract: Amides are widespread in biologically active compounds with a broad range of applications in biotechnology, agriculture and medicine. Therefore, as alternative to chemical synthesis the biocatalytic amide synthesis is a very interesting field of research. ...

Abstract	Amides are widespread in biologically active compounds with a broad range of applications in biotechnology, agriculture and medicine. Therefore, as alternative to chemical synthesis the biocatalytic amide synthesis is a very interesting field of research. As usual, Nature can serve as guide in the quest for novel biocatalysts. Several mechanisms for carboxylate activation involving mainly acyl-adenylate, acyl-phosphate or acyl-enzyme intermediates have been discovered, but also completely different pathways to amides are found. In addition to ribosomes, selected enzymes of almost all main enzyme classes are able to synthesize amides. In this review we give an overview about amide synthesis in Nature, as well as biotechnological applications of these enzymes. Moreover, several examples of biocatalytic amide synthesis are given.
MeSH term(s)	Adenosine Triphosphate ; Amides ; Biocatalysis ; Biotechnology ; Hydrolases ; Peptidyl Transferases
Chemical Substances	Amides ; Adenosine Triphosphate (8L70Q75FXE) ; Peptidyl Transferases (EC 2.3.2.12) ; Hydrolases (EC 3.-)
Language	English
Publishing date	2016-10-10
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	843647-2
ISSN	1873-4863 ; 0168-1656 ; 1389-0352
ISSN (online)	1873-4863
ISSN	0168-1656 ; 1389-0352
DOI	10.1016/j.jbiotec.2016.03.023
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2299: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Amides in Nature and Biocatalysis

Pitzer, Julia / Kerstin Steiner

Journal of biotechnology. 2016 Oct. 10, v. 235

2016

Abstract	Amides are widespread in biologically active compounds with a broad range of applications in biotechnology, agriculture and medicine. Therefore, as alternative to chemical synthesis the biocatalytic amide synthesis is a very interesting field of research. As usual, Nature can serve as guide in the quest for novel biocatalysts. Several mechanisms for carboxylate activation involving mainly acyl-adenylate, acyl-phosphate or acyl-enzyme intermediates have been discovered, but also completely different pathways to amides are found. In addition to ribosomes, selected enzymes of almost all main enzyme classes are able to synthesize amides. In this review we give an overview about amide synthesis in Nature, as well as biotechnological applications of these enzymes. Moreover, several examples of biocatalytic amide synthesis are given.
Keywords	amides ; bioactive properties ; biocatalysis ; biocatalysts ; biotechnology ; enzymes ; medicine ; ribosomes
Language	English
Dates of publication	2016-1010
Size	p. 32-46.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	843647-2
ISSN	1873-4863 ; 0168-1656 ; 1389-0352
ISSN (online)	1873-4863
ISSN	0168-1656 ; 1389-0352
DOI	10.1016/j.jbiotec.2016.03.023
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Cologne/Königswinter

Zs.A 2299: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Racemization-free and scalable amidation of l-proline in organic media using ammonia and a biocatalyst only

Pitzer, Julia / Steiner, Kerstin / Schmid, Christian / Schein, Viktor K. / Prause, Christoph / Kniely, Claudia / Reif, Michaela / Geier, Martina / Pietrich, Elena / Reiter, Tamara / Selig, Philipp / Stückler, Clemens / Pöchlauer, Peter / Steinkellner, Georg / Gruber, Karl / Schwab, Helmut / Glieder, Anton / Kroutil, Wolfgang

Green chemistry. 2022 July 4, v. 24, no. 13

2022

Abstract: Efficient amide formation is of high importance for the chemical and pharmaceutical industry. The direct biocatalytic one-pot transformation of acids into amides without substrate activation is a highly desirable but highly challenging reaction; this is ... ...

Abstract	Efficient amide formation is of high importance for the chemical and pharmaceutical industry. The direct biocatalytic one-pot transformation of acids into amides without substrate activation is a highly desirable but highly challenging reaction; this is why in general the acid is activated using additional reagents before amide formation occurs. In particular, amidation of α-amino acids is challenging and in general requires protection strategies for the amino functionality. A further challenge is the low solubility of the unprotected amino acids in organic solvents. Furthermore, the amidation process is prone to racemisation as observed for the acyl chloride derivative. These three challenges may be addressed using biocatalysis. Here the enzyme catalyzed, racemization-free amidation of unprotected l-proline with ammonia in an organic solvent is described. Comprehensive reaction, solvent and enzyme engineering allowed obtaining high l-prolinamide concentrations. For instance at 145 mM substrate concentration, 80% conversion was achieved employing an immobilized CalB variant and ammonia in 2-methyl-2-butanol at 70 °C. A two-fold increase in l-prolinamide formation was achieved employing the immobilized and engineered enzyme variant CalBopt-24 T245S compared to wild type CalB. In contrast to chemical processes, racemization, halogenated solvents and waste are avoided/minimized and atom efficiency is significantly improved from 45.5% to 86.4%. The excellent optical purity of the obtained product (ee >99%) and the stability of immobilized CalB pave the way for an innovative industrial process to produce l-prolinamide, a key intermediate in drug synthesis.
Keywords	amides ; ammonia ; biocatalysis ; biocatalysts ; drugs ; enzymes ; green chemistry ; pharmaceutical industry ; proline ; solubility ; solvents ; wastes
Language	English
Dates of publication	2022-0704
Size	p. 5171-5180.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2006274-6
ISSN	1463-9270 ; 1463-9262
ISSN (online)	1463-9270
ISSN	1463-9262
DOI	10.1039/d2gc00783e
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article ; Online: Publisher Correction: Engineered bidirectional promoters enable rapid multi-gene co-expression optimization.

Vogl, Thomas / Kickenweiz, Thomas / Pitzer, Julia / Sturmberger, Lukas / Weninger, Astrid / Biggs, Bradley W / Köhler, Eva-Maria / Baumschlager, Armin / Fischer, Jasmin Elgin / Hyden, Patrick / Wagner, Marlies / Baumann, Martina / Borth, Nicole / Geier, Martina / Ajikumar, Parayil Kumaran / Glieder, Anton

Nature communications

2021 Volume 12, Issue 1, Page(s) 1287

Language	English
Publishing date	2021-02-18
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-21369-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Synthetic core promoters for Pichia pastoris.

Vogl, Thomas / Ruth, Claudia / Pitzer, Julia / Kickenweiz, Thomas / Glieder, Anton

ACS synthetic biology

2013 Volume 3, Issue 3, Page(s) 188–191

Abstract: Synthetic promoters are commonly used tools for circuit design or high level protein production. Promoter engineering efforts in yeasts, such as Saccharomyces cerevisiae and Pichia pastoris have mostly been focused on altering upstream regulatory ... ...

Abstract	Synthetic promoters are commonly used tools for circuit design or high level protein production. Promoter engineering efforts in yeasts, such as Saccharomyces cerevisiae and Pichia pastoris have mostly been focused on altering upstream regulatory sequences such as transcription factor binding sites. In higher eukaryotes synthetic core promoters, directly needed for transcription initiation by RNA Polymerase II, have been successfully designed. Here we report the first synthetic yeast core promoter for P. pastoris, based on natural yeast core promoters. Furthermore we used this synthetic core promoter sequence to engineer the core promoter of the natural AOX1 promoter, thereby creating a set of core promoters providing a range of different expression levels. As opposed to engineering strategies of the significantly longer entire promoter, such short core promoters can directly be added on a PCR primer facilitating library generation and are sufficient to obtain variable expression yields.
MeSH term(s)	Base Sequence ; Genes, Fungal/genetics ; Genetic Engineering/methods ; Molecular Sequence Data ; Pichia/genetics ; Promoter Regions, Genetic/genetics ; Sequence Alignment ; Synthetic Biology/methods
Language	English
Publishing date	2013-11-04
Publishing country	United States
Document type	Journal Article
ISSN	2161-5063
ISSN (online)	2161-5063
DOI	10.1021/sb400091p
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Improved selectivity of an engineered multi-product terpene synthase.

Lauchli, Ryan / Pitzer, Julia / Kitto, Rebekah Z / Kalbarczyk, Karolina Z / Rabe, Kersten S

Organic & biomolecular chemistry

2014 Volume 12, Issue 23, Page(s) 4013–4020

Abstract: Mutation of the sesquiterpene synthase Cop2 was conducted with a high-throughput screen for the cyclization activity using a non-natural substrate. A mutant of Cop2 was identified that contained three amino acid substitutions. This mutant, 17H2, ... ...

Abstract	Mutation of the sesquiterpene synthase Cop2 was conducted with a high-throughput screen for the cyclization activity using a non-natural substrate. A mutant of Cop2 was identified that contained three amino acid substitutions. This mutant, 17H2, converted the natural substrate FPP into germacrene D-4-ol with 77% selectivity. This selectivity is in contrast to that of the parent enzyme in which germacrene D-4-ol is produced as 29% and α-cadinol is produced as 46% of the product mixture. The mutations were shown to each contribute to this selectivity, and a homology model suggested that the mutations lie near to the active site though would be unlikely to be targeted for mutation by rational methods. Kinetic comparisons show that 17H2 maintains a kcat/KM of 0.62 mM(-1) s(-1), which is nearly identical to that of the parent Cop2, which had a kcat/KM of 0.58 mM(-1) s(-1).
MeSH term(s)	Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/metabolism ; Amino Acid Sequence ; Biocatalysis ; Coprinus/enzymology ; Gas Chromatography-Mass Spectrometry ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Polyisoprenyl Phosphates/chemistry ; Polyisoprenyl Phosphates/metabolism ; Protein Engineering ; Sequence Alignment ; Sesquiterpenes/chemistry ; Sesquiterpenes/metabolism ; Structural Homology, Protein ; Substrate Specificity
Chemical Substances	Polyisoprenyl Phosphates ; Sesquiterpenes ; farnesyl pyrophosphate (79W6B01D07) ; Alkyl and Aryl Transferases (EC 2.5.-) ; terpene synthase (EC 2.5.1.-)
Language	English
Publishing date	2014-06-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2097583-1
ISSN	1477-0539 ; 1477-0520
ISSN (online)	1477-0539
ISSN	1477-0520
DOI	10.1039/c4ob00479e
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Enzymes revolutionize the bioproduction of value-added compounds: From enzyme discovery to special applications.

Wiltschi, Birgit / Cernava, Tomislav / Dennig, Alexander / Galindo Casas, Meritxell / Geier, Martina / Gruber, Steffen / Haberbauer, Marianne / Heidinger, Petra / Herrero Acero, Enrique / Kratzer, Regina / Luley-Goedl, Christiane / Müller, Christina A / Pitzer, Julia / Ribitsch, Doris / Sauer, Michael / Schmölzer, Katharina / Schnitzhofer, Wolfgang / Sensen, Christoph W / Soh, Jung /

Steiner, Kerstin / Winkler, Christoph K / Winkler, Margit / Wriessnegger, Tamara

Biotechnology advances

2020 Volume 40, Page(s) 107520

Abstract: Competitive sustainable production in industry demands new and better biocatalysts, optimized bioprocesses and cost-effective product recovery. Our review sheds light on the progress made for the individual steps towards these goals, starting with the ... ...

Abstract	Competitive sustainable production in industry demands new and better biocatalysts, optimized bioprocesses and cost-effective product recovery. Our review sheds light on the progress made for the individual steps towards these goals, starting with the discovery of new enzymes and their corresponding genes. The enzymes are subsequently engineered to improve their performance, combined in reaction cascades to expand the reaction scope and integrated in whole cells to provide an optimal environment for the bioconversion. Strain engineering using synthetic biology methods tunes the host for production, reaction design optimizes the reaction conditions and downstream processing ensures the efficient recovery of commercially viable products. Selected examples illustrate how modified enzymes can revolutionize future-oriented applications ranging from the bioproduction of bulk-, specialty- and fine chemicals, active pharmaceutical ingredients and carbohydrates, over the conversion of the greenhouse-gas CO
MeSH term(s)	Biocatalysis ; Enzymes ; Organic Chemicals ; Synthetic Biology
Chemical Substances	Enzymes ; Organic Chemicals
Language	English
Publishing date	2020-01-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	47165-3
ISSN	1873-1899 ; 0734-9750
ISSN (online)	1873-1899
ISSN	0734-9750
DOI	10.1016/j.biotechadv.2020.107520
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3730: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Publisher Correction: Engineered bidirectional promoters enable rapid multi-gene co-expression optimization.

Nature communications

2018 Volume 9, Issue 1, Page(s) 4566

Abstract: The original version of this Article was updated after publication to add the ORCID ID of the author Thomas Vogl, which was inadvertently omitted, and to include a corrected version of the 'Description of Additional Supplementary Files' which originally ... ...

Abstract	The original version of this Article was updated after publication to add the ORCID ID of the author Thomas Vogl, which was inadvertently omitted, and to include a corrected version of the 'Description of Additional Supplementary Files' which originally lacked legends for each file.
Language	English
Publishing date	2018-10-29
Publishing country	England
Document type	Journal Article ; Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-018-07112-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Engineered bidirectional promoters enable rapid multi-gene co-expression optimization.

Nature communications

2018 Volume 9, Issue 1, Page(s) 3589

Abstract: Numerous synthetic biology endeavors require well-tuned co-expression of functional components for success. Classically, monodirectional promoters (MDPs) have been used for such applications, but MDPs are limited in terms of multi-gene co-expression ... ...

Abstract	Numerous synthetic biology endeavors require well-tuned co-expression of functional components for success. Classically, monodirectional promoters (MDPs) have been used for such applications, but MDPs are limited in terms of multi-gene co-expression capabilities. Consequently, there is a pressing need for new tools with improved flexibility in terms of genetic circuit design, metabolic pathway assembly, and optimization. Here, motivated by nature's use of bidirectional promoters (BDPs) as a solution for efficient gene co-expression, we generate a library of 168 synthetic BDPs in the yeast Komagataella phaffii (syn. Pichia pastoris), leveraging naturally occurring BDPs as a parts repository. This library of synthetic BDPs allows for rapid screening of diverse expression profiles and ratios to optimize gene co-expression, including for metabolic pathways (taxadiene, β-carotene). The modular design strategies applied for creating the BDP library could be relevant in other eukaryotic hosts, enabling a myriad of metabolic engineering and synthetic biology applications.
MeSH term(s)	Alkenes/metabolism ; Cytochrome P-450 CYP2D6/genetics ; Diterpenes/metabolism ; Farnesyltranstransferase/genetics ; Gene Expression Regulation, Fungal ; Genetic Engineering/methods ; Histones/genetics ; Microorganisms, Genetically-Modified ; Pichia/genetics ; Pichia/metabolism ; Promoter Regions, Genetic ; beta Carotene/genetics ; beta Carotene/metabolism
Chemical Substances	Alkenes ; Diterpenes ; Histones ; taxa-4(5),11(12)diene ; beta Carotene (01YAE03M7J) ; Cytochrome P-450 CYP2D6 (EC 1.14.14.1) ; Farnesyltranstransferase (EC 2.5.1.29)
Language	English
Publishing date	2018-09-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-018-05915-w
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A Toolbox of Diverse Promoters Related to Methanol Utilization: Functionally Verified Parts for Heterologous Pathway Expression in Pichia pastoris.

Vogl, Thomas / Sturmberger, Lukas / Kickenweiz, Thomas / Wasmayer, Richard / Schmid, Christian / Hatzl, Anna-Maria / Gerstmann, Michaela A / Pitzer, Julia / Wagner, Marlies / Thallinger, Gerhard G / Geier, Martina / Glieder, Anton

ACS synthetic biology

2016 Volume 5, Issue 2, Page(s) 172–186

Abstract: The heterologous expression of biosynthetic pathways for pharmaceutical or fine chemical production requires suitable expression hosts and vectors. In eukaryotes, the pathway flux is typically balanced by stoichiometric fine-tuning of reaction steps by ... ...

Abstract	The heterologous expression of biosynthetic pathways for pharmaceutical or fine chemical production requires suitable expression hosts and vectors. In eukaryotes, the pathway flux is typically balanced by stoichiometric fine-tuning of reaction steps by varying the transcript levels of the genes involved. Regulated (inducible) promoters are desirable to allow a separation of pathway expression from cell growth. Ideally, the promoter sequences used should not be identical to avoid loss by recombination. The methylotrophic yeast Pichia pastoris is a commonly used protein production host, and single genes have been expressed at high levels using the methanol-inducible, strong, and tightly regulated promoter of the alcohol oxidase 1 gene (PAOX1). Here, we have studied the regulation of the P. pastoris methanol utilization (MUT) pathway to identify a useful set of promoters that (i) allow high coexpression and (ii) differ in DNA sequence to increase genetic stability. We noticed a pronounced involvement of the pentose phosphate pathway (PPP) and genes involved in the defense of reactive oxygen species (ROS), providing strong promoters that, in part, even outperform PAOX1 and offer novel regulatory profiles. We have applied these tightly regulated promoters together with novel terminators as useful tools for the expression of a heterologous biosynthetic pathway. With the synthetic biology toolbox presented here, P. pastoris is now equipped with one of the largest sets of strong and co-regulated promoters of any microbe, moving it from a protein production host to a general industrial biotechnology host.
MeSH term(s)	Gene Expression Regulation, Fungal/drug effects ; Methanol/pharmacokinetics ; Pichia/genetics ; Pichia/metabolism ; Promoter Regions, Genetic ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics
Chemical Substances	Recombinant Proteins ; Methanol (Y4S76JWI15)
Language	English
Publishing date	2016-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2161-5063
ISSN (online)	2161-5063
DOI	10.1021/acssynbio.5b00199
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED