The biosynthesis of thiamine. A yeast enzyme system which converts 2-methyl-4-amino-5-aminomethylpyridimine to 2-methyl-4-amino-5-hydroxymethylpyrimidine

R. Wei; Lawrence Lewin

doi:10.1016/0304-4165(71)90210-8

The biosynthesis of thiamine. A yeast enzyme system which converts 2-methyl-4-amino-5-aminomethylpyridimine to 2-methyl-4-amino-5-hydroxymethylpyrimidine

R. Wei^*, Lawrence Lewin

^*Corresponding author for this work

Georgetown University

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

1. 1. An enzyme sysetm obtained from baker's yeast converted 2-methyl-4 amino-5-aminomethylpyrimidine to 2-methyl-4-amino-5-hydroxymethylpyrimidine, a known intermediate in thiamine biosynthesis. The pH optimum of the system was 7.8 and the apparent K_m value for the substrate was 5·10^-5 M. The enzyme system was inhibited by 2-mercaptoethanol, pyridoxal phosphate, the amine oxidase inhibitors pargyline and tranylcypromine, and by various carbonyl reagents and chelating agents. 2. 2. Enzymes systems catalyzing a similar reaction were reaction were found to be present in Neurospora crasa extracts and in a crude preparation of Bacillus thiaminolyticus thiaminase.

Original language	English
Pages (from-to)	253-257
Number of pages	5
Journal	Biochimica et Biophysica Acta - General Subjects
Volume	230
Issue number	2
DOIs	https://doi.org/10.1016/0304-4165(71)90210-8
State	Published - 23 Feb 1971
Externally published	Yes

Funding

Funders	Funder number
Washington Heart Association
U.S. Public Health Service	AMo8393

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10.1016/0304-4165(71)90210-8

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title = "The biosynthesis of thiamine. A yeast enzyme system which converts 2-methyl-4-amino-5-aminomethylpyridimine to 2-methyl-4-amino-5-hydroxymethylpyrimidine",

abstract = "1. 1. An enzyme sysetm obtained from baker's yeast converted 2-methyl-4 amino-5-aminomethylpyrimidine to 2-methyl-4-amino-5-hydroxymethylpyrimidine, a known intermediate in thiamine biosynthesis. The pH optimum of the system was 7.8 and the apparent Km value for the substrate was 5·10-5 M. The enzyme system was inhibited by 2-mercaptoethanol, pyridoxal phosphate, the amine oxidase inhibitors pargyline and tranylcypromine, and by various carbonyl reagents and chelating agents. 2. 2. Enzymes systems catalyzing a similar reaction were reaction were found to be present in Neurospora crasa extracts and in a crude preparation of Bacillus thiaminolyticus thiaminase.",

author = "R. Wei and Lawrence Lewin",

note = "Funding Information: This work was supported by U.S. Public Health Service Grant AMo8393 and by a grant from ttle Washington Heart Association.",

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doi = "10.1016/0304-4165(71)90210-8",

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AU - Lewin, Lawrence

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AB - 1. 1. An enzyme sysetm obtained from baker's yeast converted 2-methyl-4 amino-5-aminomethylpyrimidine to 2-methyl-4-amino-5-hydroxymethylpyrimidine, a known intermediate in thiamine biosynthesis. The pH optimum of the system was 7.8 and the apparent Km value for the substrate was 5·10-5 M. The enzyme system was inhibited by 2-mercaptoethanol, pyridoxal phosphate, the amine oxidase inhibitors pargyline and tranylcypromine, and by various carbonyl reagents and chelating agents. 2. 2. Enzymes systems catalyzing a similar reaction were reaction were found to be present in Neurospora crasa extracts and in a crude preparation of Bacillus thiaminolyticus thiaminase.

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The biosynthesis of thiamine. A yeast enzyme system which converts 2-methyl-4-amino-5-aminomethylpyridimine to 2-methyl-4-amino-5-hydroxymethylpyrimidine

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