(Q38290178)

English

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

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scholarly article

1 reference

Europe PubMed Central

1 September 2017

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 (English)

1 reference

Europe PubMed Central

1 September 2017

Sorghum bicolor

1 reference

1 reference

author name string

Koch BM

1

1 reference

Europe PubMed Central

1 September 2017

Sibbesen O

2

1 reference

Europe PubMed Central

1 September 2017

Halkier BA

3

1 reference

Europe PubMed Central

1 September 2017

Svendsen I

4

1 reference

Europe PubMed Central

1 September 2017

Møller BL

5

1 reference

Europe PubMed Central

1 September 2017

language of work or name

0 references

publication date

1 October 1995

1 reference

Europe PubMed Central

1 September 2017

Archives of Biochemistry and Biophysics

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Europe PubMed Central

1 September 2017

323

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Europe PubMed Central

1 September 2017

1

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Europe PubMed Central

1 September 2017

177-186

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Europe PubMed Central

1 September 2017

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Substrate specificities and functions of the P450 cytochromes

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Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea

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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.

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Localization of Cinnamic Acid 4-Monooxygenase and the Membrane-bound Enzyme System for Dhurrin Biosynthesis in Sorghum Seedlings

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Secondary structure prediction of 52 membrane-bound cytochromes P450 shows a strong structural similarity to P450cam

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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

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Cloning of eggplant hypocotyl cDNAs encoding cytochromes P450 belonging to a novel family (CYP77).

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Purification and characterization of recombinant cytochrome P450TYR expressed at high levels in Escherichia coli.

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Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible forms of rabbit liver microsomal cytochrome P-450.

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A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence.

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Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines

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Multiple forms of plant cytochromes p-450.

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Minipreps of DNA from bacteriophage lambda

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Sequence analysis of ripening-related cytochrome P-450 cDNAs from avocado fruit

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Isolation and sequence of a cDNA encoding the Jerusalem artichoke cinnamate 4-hydroxylase, a major plant cytochrome P450 involved in the general phenylpropanoid pathway

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Primary and secondary structural patterns in eukaryotic cytochrome P-450 families correspond to structures of the helix-rich domain of Pseudomonas putida cytochrome P-450cam. Indications for a similar overall topology

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Molecular evolution of P450 superfamily and P450-containing monooxygenase systems

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A comprehensive set of sequence analysis programs for the VAX

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Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase

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Importance of the proline-rich region following signal-anchor sequence in the formation of correct conformation of microsomal cytochrome P-450s

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The cloning of eggplant seedling cDNAs encoding proteins from a novel cytochrome P-450 family (CYP76).

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Molecular cloning of an allene oxide synthase: a cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides

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Identifiers

10.1006/ABBI.1995.0024

1 reference

Europe PubMed Central

1 September 2017

1 reference

Europe PubMed Central

1 September 2017

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