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Literature summary extracted from

  • Nishimune, T.; Watanabe, Y.; Okazaki, H.
    Studies on the polymorphism of thiaminase I in seawater fish (2008), J. Nutr. Sci. Vitaminol., 54, 339-346.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.2 Cd2+ the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes Fistularia petimba

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.2 Cd2+ weak activation with thiamine and aniline as substrates Fistularia petimba

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.2 106000
-
 pI 5.7 isoenzyme, gel filtration Fistularia petimba

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.2 thiamine + pyridine Fistularia petimba
-
 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.2 Fistularia petimba
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.2 pI 5.7 isoenzyme Fistularia petimba

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.2 liver
-
 Fistularia petimba
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.2 thiamine + 2-mercaptoethanol
-
 Fistularia petimba ?
-
 ?
2.5.1.2 thiamine + 3-aminopyridine
-
 Fistularia petimba ?
-
 ?
2.5.1.2 thiamine + 4-aminopyridine
-
 Fistularia petimba ?
-
 ?
2.5.1.2 thiamine + aniline
-
 Fistularia petimba 5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
 ?
2.5.1.2 thiamine + cysteine
-
 Fistularia petimba ?
-
 ?
2.5.1.2 thiamine + L-lysine
-
 Fistularia petimba ?
-
 ?
2.5.1.2 thiamine + pyridine
-
 Fistularia petimba 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
 ?
2.5.1.2 thiamine + pyridine the reaction rate measured by pyridine as the second substrate is three times higher in pI 7-9 enzymes compared with pI 5.7 enzyme Fistularia petimba 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
 ?
2.5.1.2 thiamine + pyridoxine
-
 Fistularia petimba ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.2 More the purified preparation of the pI 5.7 isoenzyme gives an active 25 kDa subfragment by SDS-PAGE, together with a 15 kDa non-active subfragment. The enzyme is, thus, inferred to contain active subfragments together with the 15 kDa non-active fragments. Amino acid sequencing of the 25 kDa active subfragment reveals, together with the fully processed N-terminal sequence, two N-terminal peptides with extra Pro-Ser and Gly-Pro-Ser attached to it Fistularia petimba

Synonyms

EC Number Synonyms Comment Organism
2.5.1.2 thiaminase I
-
 Fistularia petimba

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.2 45
-
 pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + 2-mercaptoethanol Fistularia petimba
2.5.1.2 45 55 pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + aniline Fistularia petimba

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.2 7.8
-
 pI 7-9 isoenzym, thiamine + 2-mercaptoethanol Fistularia petimba
2.5.1.2 8.2
-
 pI 5.7 isoenzyme, thiamine + 2-mercaptoethanol Fistularia petimba
2.5.1.2 8.2
-
 pI 5.7 isoenzyme, thiamine + aniline Fistularia petimba

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.5.1.2 Fistularia petimba the liver of Fisturalia petimba contains thiaminase I of at least three different pIs and the major fraction exhibits pI 5.7. The most evident difference among pI isozymes is the size of the active subfragments into which they are dissociated. pI 5.7 enzyme dissociates into subfragments of 25 kDa, while pI 7-9 enzymes dissociates into approximately 22000 Da. The reaction rate measured by pyridine as the second substrate is three times higher in pI 7-9 enzymes compared with pI 5.7 enzyme. The degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
-
 5.7