BRENDA - Enzyme Database show
show all sequences of 2.5.1.2

Studies on the polymorphism of thiaminase I in seawater fish

Nishimune, T.; Watanabe, Y.; Okazaki, H.; J. Nutr. Sci. Vitaminol. 54, 339-346 (2008)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cd2+
the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
Fistularia petimba
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cd2+
weak activation with thiamine and aniline as substrates
Fistularia petimba
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
106000
-
pI 5.7 isoenzyme, gel filtration
Fistularia petimba
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thiamine + pyridine
Fistularia petimba
-
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Fistularia petimba
-
-
-
Purification (Commentary)
Commentary
Organism
pI 5.7 isoenzyme
Fistularia petimba
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Fistularia petimba
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thiamine + 2-mercaptoethanol
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + 3-aminopyridine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + 4-aminopyridine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + aniline
-
699702
Fistularia petimba
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + cysteine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + L-lysine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + pyridine
-
699702
Fistularia petimba
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
-
?
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
699702
Fistularia petimba
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
-
?
thiamine + pyridoxine
-
699702
Fistularia petimba
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
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
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
55
pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + aniline
Fistularia petimba
45
-
pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + 2-mercaptoethanol
Fistularia petimba
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
pI 7-9 isoenzym, thiamine + 2-mercaptoethanol
Fistularia petimba
8.2
-
pI 5.7 isoenzyme, thiamine + 2-mercaptoethanol; pI 5.7 isoenzyme, thiamine + aniline
Fistularia petimba
pI Value
Organism
Commentary
pI Value Maximum
pI Value
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
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cd2+
the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
Fistularia petimba
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cd2+
weak activation with thiamine and aniline as substrates
Fistularia petimba
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
106000
-
pI 5.7 isoenzyme, gel filtration
Fistularia petimba
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thiamine + pyridine
Fistularia petimba
-
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
pI 5.7 isoenzyme
Fistularia petimba
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Fistularia petimba
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thiamine + 2-mercaptoethanol
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + 3-aminopyridine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + 4-aminopyridine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + aniline
-
699702
Fistularia petimba
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + cysteine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + L-lysine
-
699702
Fistularia petimba
?
-
-
-
?
thiamine + pyridine
-
699702
Fistularia petimba
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
-
?
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
699702
Fistularia petimba
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
-
?
thiamine + pyridoxine
-
699702
Fistularia petimba
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
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
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
55
pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + aniline
Fistularia petimba
45
-
pI 5.7 isoenzyme, pI 7-9 isoenzym, thiamine + 2-mercaptoethanol
Fistularia petimba
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
pI 7-9 isoenzym, thiamine + 2-mercaptoethanol
Fistularia petimba
8.2
-
pI 5.7 isoenzyme, thiamine + 2-mercaptoethanol; pI 5.7 isoenzyme, thiamine + aniline
Fistularia petimba
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
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
Other publictions for EC 2.5.1.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737986
Lau
Metabolomic profiling of Burkh ...
Burkholderia pseudomallei, Burkholderia thailandensis
Cell Biosci.
5
26
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
738782
Blakeslee
-
Thiaminase activity in native ...
Elliptio complanata, Strophitus undulatus
J. Great Lakes Res.
41
516-519
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739509
Kraft
A rapid method for assaying th ...
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus 8103
PLoS ONE
9
e92688
2014
-
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
737686
Sikowitz
Structure of a Clostridium bot ...
Clostridium botulinum
Biochemistry
52
7830-7839
2013
-
-
-
1
6
-
-
6
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
1
6
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
6
6
723037
Liu
Pharmacologic properties of po ...
Paenibacillus thiaminolyticus
J. Pharmacol. Exp. Ther.
341
775-783
2012
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711655
Liu
Sensitivity of breast cancer c ...
Paenibacillus thiaminolyticus
Cancer Chemother. Pharmacol.
66
171-179
2010
-
1
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
704238
Wistbacka
Thiaminase activity of crucian ...
Carassius carassius
J. Aquat. Anim. Health
21
217-228
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
685198
Soriano
Structural similarities betwee ...
Paenibacillus thiaminolyticus
Biochemistry
47
1346-1357
2008
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688111
Wistbacka
-
Thiaminase activity of Baltic ...
Clupea harengus, Gasterosteus aculeatus, Sprattus sprattus
J. Fish Biol.
72
787-802
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
699702
Nishimune
Studies on the polymorphism of ...
Fistularia petimba
J. Nutr. Sci. Vitaminol.
54
339-346
2008
-
-
-
-
-
-
1
-
-
1
1
1
-
4
-
-
1
-
-
1
-
-
9
1
2
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
1
1
-
-
-
1
-
1
-
-
9
1
2
-
-
-
2
-
-
1
-
-
-
-
-
-
684401
Hanes
An assay for thiaminase I in c ...
Paenibacillus thiaminolyticus
Anal. Biochem.
368
33-38
2007
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
1
-
2
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
2
-
2
-
-
-
-
4
1
-
-
-
-
-
-
-
2
2
636861
Wistbacka
-
Thiaminase activity of gastroi ...
Clupea harengus, Salmo salar
J. Fish Biol.
60
1031-1042
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636859
Wu
-
Mechanistic studies on thiamin ...
Paenibacillus thiaminolyticus
Bioorg. Chem.
28
45-48
2000
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636860
Bos
Some molecular and enzymatic p ...
Cyprinus carpio
J. Protein Chem.
19
75-84
2000
-
-
-
-
-
-
-
-
1
-
1
-
-
2
-
-
1
-
-
2
-
-
20
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
2
-
-
20
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
636858
Campobasso
Crystallization and preliminar ...
Paenibacillus thiaminolyticus
Acta Crystallogr. Sect. D
54
448-450
1998
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
636854
Kelleher
Identification of modification ...
Paenibacillus thiaminolyticus
J. Biol. Chem.
272
32215-32220
1997
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636853
Costello
Mechanistic studies on thiamin ...
Paenibacillus thiaminolyticus
J. Biol. Chem.
271
3445-3452
1996
-
-
1
-
1
-
1
1
-
-
1
-
-
3
1
-
1
-
-
1
-
-
1
1
1
-
-
-
-
-
1
-
1
-
-
-
-
1
-
-
1
-
-
1
1
1
-
-
1
-
-
1
-
1
-
1
-
-
1
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
636857
Ruml
-
Purification of thiaminase I f ...
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus DBM 1068
Potravinarske Vedy
13
181-187
1995
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636856
Sato
-
Subcellular localization of th ...
Cyprinus carpio
Comp. Biochem. Physiol. A
108A
31-38
1994
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636855
Fabre
-
Thiaminase activity in Equiset ...
Equisetum arvense
Plant. Med. Phytother.
26
190-197
1993
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
1
2
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
2
-
-
1
-
-
-
-
-
-
-
-
-
636852
Hutter
Inhibition of thiaminase I fro ...
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus BMM
Biochemistry
26
1969-1973
1987
-
-
-
-
-
-
3
-
1
-
-
-
-
4
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
1
-
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636847
Boyd
Studies on thiaminase I activi ...
Megasphaera elsdenii
J. Agric. Sci.
104
637-642
1985
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
636851
McCleary
-
The purification and propertie ...
Cheilanthes sieberi, Marsilea angustifolia, Marsilea drummondii, Marsilea mutica, Pteridium esculentum, Velesunio ambiguus
Phytochemistry
16
207-213
1977
4
-
-
-
-
-
17
49
-
1
4
5
-
6
-
-
1
-
-
8
-
-
41
-
-
-
-
-
4
4
4
-
-
-
-
4
-
-
-
-
-
-
-
17
-
49
-
1
4
5
-
-
-
1
-
8
-
-
41
-
-
-
-
-
4
4
4
-
-
-
-
-
-
-
636849
Suzuki
Reversible inactivation of ext ...
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus YUSM I00I
Biochim. Biophys. Acta
293
111-117
1973
7
-
-
-
-
-
7
-
1
-
-
-
-
3
-
-
-
-
-
1
-
-
6
-
-
1
-
-
-
-
1
-
-
-
-
7
-
-
-
-
-
-
-
7
-
-
1
-
-
-
-
-
-
-
-
1
-
-
6
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
636850
Agee
Reversible inactivation of thi ...
Paenibacillus thiaminolyticus
J. Bacteriol.
115
957-965
1973
2
-
-
-
-
-
2
-
1
-
-
-
-
2
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
1
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
636848
Suzuki
Reversible inactivation of cel ...
Paenibacillus thiaminolyticus
J. Biochem.
72
1053-1055
1972
-
-
-
-
-
-
3
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
636846
Wittliff
The extracellular thiaminase I ...
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus M
Biochemistry
7
736-744
1968
-
-
-
-
-
-
2
2
1
-
1
-
-
3
-
-
1
-
-
1
-
-
2
-
1
2
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
1
-
1
-
-
-
-
1
-
1
-
-
2
-
1
2
-
-
-
1
1
-
-
-
-
-
-
-
636845
Fujita
Thiaminase ...
Acanthogobius flavimanus, Anadara inflata, Aneurinibacillus aneurinilyticus, Aneurinibacillus aneurinilyticus BKA, Anguilla japonica, Athyrium nipponicum, Auxis hira, Carassius auratus, Celosia crista, Charybdis 6-dentata, Circe scripta, Clava kochi, Corbicula leana, Cristaria plicata, Cyprinus carpio, Dicranopteris linearis, Dicranopteris sp., Dryopteris erythrosora, Dryopteris lacera, Eleotris oxycephala, Equisetum arvense, Eviota abax, Gnathopogon mayedae, Haliotis gigantea, Haliotis japonica, Hypomesus olidus, Ischikauia steenackeri, Leptochilus ellipticus, Leucopsarion petersii, Lycopodium clavatum, Mactra quadrangularis, Mactra sulcataria, Meretrix meretrix, Misgurnus anguillicaudatus, Mugil cephalus, no activity in Astroconger myriaster, no activity in Cambaroides japonicus, no activity in Camposcia retusa, no activity in Metapenaeopsis acclivis, no activity in Plecoglossus altivelis, no activity in Squilla oratoria, Odontobutis obscura, Osmunda japonica, Ostrea laperousei, Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus BMM, Panulirus japonicus, Paphia philippinarum, Polystichum aculeatum, Polystichum falcatum, Polystichum fortunei, Polystichum tsus-simense, Portunus trituberculatus, Pteridium aquilinum, Rhinogobius similis, Silurus asotus, Solen gouldi, Struthiopteris niponica, Thiara libertina, Turbo cornutus, Umbonium costatum, Viviparus malleatus
Adv. Enzymol. Relat. Subj. Biochem.
15
389-421
1954
29
4
-
-
-
-
25
-
-
-
-
-
-
63
-
-
-
-
-
99
-
-
5
-
-
9
-
-
9
-
-
-
-
-
-
29
4
-
-
-
-
-
-
25
-
-
-
-
-
-
-
-
-
-
-
99
-
-
5
-
-
9
-
-
9
-
-
-
-
-
-
-
-
-