UB Paderborn / Katalog / Suche / in CDI

Potential role of glycosidase inhibitors in industrial biotechnological applications

BBA - Proteins and Proteomics, 2004-02, Vol.1696 (2), p.275-287

2004

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Mapping of residues involved in the interaction between the Bacillus subtilis xylanase A and proteinaceous wheat xylanase inhibitors

Protein engineering, design and selection, 2006-05, Vol.19 (5), p.205-210

2006

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Cytochrome P-450(TYR) is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

The Journal of biological chemistry, 1995-02, Vol.270 (8), p.3506

1995

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Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Proceedings of the National Academy of Sciences - PNAS, 1994-10, Vol.91 (21), p.9740-9744

1994

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Metabolism of carotenoids and apocarotenoids during ripening of raspberry fruit

BioFactors (Oxford), 2008, Vol.34 (1), p.57-66

2008

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Behaviour of family 10 and 11 xylanases towards arabinoxylans with varying structure

Journal of the science of food and agriculture, 2006-08, Vol.86 (11), p.1618-1622

2006

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Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

The Journal of biological chemistry, 1995-02, Vol.270 (8), p.3506-3511

1995

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The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Archives of biochemistry and biophysics, 1995-10, Vol.323 (1), p.177-186

1995

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Isolation of plant and recombinant CYP79

1991

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Isolation of the heme-thiolate enzyme cytochrome P-450(TYR), which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Proceedings of the National Academy of Sciences - PNAS, 1994-10, Vol.91 (21), p.9740

1994

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Cytochrome P450cam substrate specificity: relationship between structure and catalytic oxidation of alkylbenzenes

Archives of biochemistry and biophysics, 1998-05, Vol.353 (2), p.285-296

1998

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Structure-function of cytochromes P450 and flavin-containing monooxygenases: implications for drug metabolism

Drug metabolism and disposition, 1998-12, Vol.26 (12), p.1223

1998

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Putidaredoxin reductase-putidaredoxin-cytochrome p450cam triple fusion protein. Construction of a self-sufficient Escherichia coli catalytic system

The Journal of biological chemistry, 1996-09, Vol.271 (37), p.22462-22469

1996

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The substrate specificity of cytochrome P450cam

Bioorganic & medicinal chemistry, 1998-09, Vol.6 (9), p.1501-1508

1998

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[30] Isolation of plant and recombinant CYP79

Methods in Enzymology, 1996, Vol.272, p.268-274

1996

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Putidaredoxin reductase-putidaredoxin-cytochrome P450 sub(cam) triple fusion protein. Construction of a self-sufficient Escherichia coli catalytic system

The Journal of biological chemistry, 1996-01, Vol.271 (37), p.22462-22469

1996

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9.8: Purification, cloning and expression of a multifunctional cytochrome P450 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Physiologia plantarum, 1994-07, Vol.91 (3)

1994

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9.5: Electron donation from cytochrome B, to a cytochrome P450 enzyme catalyzing dhurrin biosynthesis in Sorghum bicolor [cyanogenic glucosides]

Physiologia plantarum, 1994-07, Vol.91 (3)

1994

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Microbial production of natural raspbery ketone

Biotechnology journal, 2007, Vol.2 (10)

2007

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Characterization of cytochrome P450TYR, a multifunctional haem-thiolate N-hydroxylase involved in the biosynthesis of the cyanogenic glucoside dhurrin

Drug metabolism and drug interactions, 1995, Vol.12 (3-4), p.285

1995

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Pangenome graph construction from genome alignments with Minigraph-Cactus

Nature biotechnology, 2024-04, Vol.42 (4), p.663-673

2024

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Recombination between heterologous human acrocentric chromosomes

Nature (London), 2023-05, Vol.617 (7960), p.335-343

2023

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Increased mutation and gene conversion within human segmental duplications

Nature (London), 2023-05, Vol.617 (7960), p.325-334

2023

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Pan-conserved segment tags identify ultra-conserved sequences across assemblies in the human pangenome

Cell reports methods, 2023-08, Vol.3 (8), p.100543-100543, Article 100543

2023

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Potential role of glycosidase inhibitors in industrial biotechnological applications

Mapping of residues involved in the interaction between the Bacillus subtilis xylanase A and proteinaceous wheat xylanase inhibitors

Cytochrome P-450(TYR) is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Metabolism of carotenoids and apocarotenoids during ripening of raspberry fruit

Behaviour of family 10 and 11 xylanases towards arabinoxylans with varying structure

Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Isolation of plant and recombinant CYP79

Isolation of the heme-thiolate enzyme cytochrome P-450(TYR), which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

Cytochrome P450cam substrate specificity: relationship between structure and catalytic oxidation of alkylbenzenes

Structure-function of cytochromes P450 and flavin-containing monooxygenases: implications for drug metabolism

Putidaredoxin reductase-putidaredoxin-cytochrome p450cam triple fusion protein. Construction of a self-sufficient Escherichia coli catalytic system

The substrate specificity of cytochrome P450cam

[30] Isolation of plant and recombinant CYP79

Putidaredoxin reductase-putidaredoxin-cytochrome P450 sub(cam) triple fusion protein. Construction of a self-sufficient Escherichia coli catalytic system

9.8: Purification, cloning and expression of a multifunctional cytochrome P450 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

9.5: Electron donation from cytochrome B, to a cytochrome P450 enzyme catalyzing dhurrin biosynthesis in Sorghum bicolor [cyanogenic glucosides]

Microbial production of natural raspbery ketone

Characterization of cytochrome P450TYR, a multifunctional haem-thiolate N-hydroxylase involved in the biosynthesis of the cyanogenic glucoside dhurrin

Pangenome graph construction from genome alignments with Minigraph-Cactus

Recombination between heterologous human acrocentric chromosomes

Increased mutation and gene conversion within human segmental duplications

Pan-conserved segment tags identify ultra-conserved sequences across assemblies in the human pangenome

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