2.4.2.60: cysteine-dependent adenosine diphosphate thiazole synthase
This is an abbreviated version!
For detailed information about cysteine-dependent adenosine diphosphate thiazole synthase, go to the full flat file.
Reaction
Synonyms
ADP-thiazole synthase, CyPBP37, NCU06110, Thi-4, THI1, Thi4
ECTree
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General Information
General Information on EC 2.4.2.60 - cysteine-dependent adenosine diphosphate thiazole synthase
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metabolism
physiological function
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an enzyme deletion mutant displays increased sensitivity to oxidative stress and enhanced thiamine diphosphate biosynthesis as compared with the wild-type strain
physiological function
enzyme is able to functionally replace Thi4 in yeast thiazole synthesis. CyPBP37 is a substrate of the chaperone activity of its own binding partner cyclophilin CyP41
physiological function
expression of Thi1 rescues a yeast Thi4 mutant when fused to the yeast Thi4 signal peptide
physiological function
protein Thi4 from Saccharomyces cerevisiae fails to catalyze the formation of the thiazole moiety from cysteine (or sulfide), glycine and a variety of C5 carbohydrates. Thi4 also fails to complement an Escherichia coli thiazole biosynthetic mutant ThiF. The ADP adduct of 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid is present at the active site of Thi4 and the carboxylic acid of the thiazole forms hydrogen bonding and electrostatic interactions with Arg301
physiological function
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enzyme without active-site Cys is the major enzyme type in developing grains that saves substantial energy during the grain-filling period
physiological function
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enzyme without active-site Cys is the major enzyme type in developing grains that saves substantial energy during the grain-filling period
physiological function
-
enzyme without active-site Cys is the major enzyme type in developing grains that saves substantial energy during the grain-filling period
physiological function
-
enzyme without active-site Cys is the major enzyme type in developing grains that saves substantial energy during the grain-filling period
physiological function
-
protein Thi4 from Saccharomyces cerevisiae fails to catalyze the formation of the thiazole moiety from cysteine (or sulfide), glycine and a variety of C5 carbohydrates. Thi4 also fails to complement an Escherichia coli thiazole biosynthetic mutant ThiF. The ADP adduct of 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid is present at the active site of Thi4 and the carboxylic acid of the thiazole forms hydrogen bonding and electrostatic interactions with Arg301
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physiological function
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enzyme is able to functionally replace Thi4 in yeast thiazole synthesis. CyPBP37 is a substrate of the chaperone activity of its own binding partner cyclophilin CyP41
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