BRENDA - Enzyme Database
show all sequences of 4.3.1.B2

Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex

Beismann-Driemeyer, S.; Sterner, R.; J. Biol. Chem. 276, 20387-20396 (2001)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli
Thermotoga maritima
Engineering
Protein Variants
Commentary
Organism
C9A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
D11N
mutation in subunit HisF. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
Thermotoga maritima
D130N
the kcat value is reduced by a factor of about 400-500, and the Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is increased almost 20fold. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
Thermotoga maritima
D176N
mutation in subunit HisF. The variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
Thermotoga maritima
D183N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
D51N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
K19S
mutation in subunit HisF. The ammonia-dependent reactions of isolated subunit HisF_K19S is similarly efficient as that of wild-type HisF. The efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired
Thermotoga maritima
additional information
eight conserved amino acids at the putative active site of subunit HisF are exchanged by site-directed mutagenesis, and the purified variants are investigated by steady state kinetics. Aspartate 11 appears to be essential for the synthase activity both in vitro and in vivo, and aspartate 130 can be partially replaced only by glutamate
Thermotoga maritima
N103A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
0.32
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
Organism
Organism
UniProt
Commentary
Textmining
Thermotoga maritima
Q9X0C8 and Q9X0C6
Q9X0C8: subunit HisH, Q9X0C6: subunit HisF
-
Thermotoga maritima DSM 3109
Q9X0C8 and Q9X0C6
Q9X0C8: subunit HisH, Q9X0C6: subunit HisF
-
Purification (Commentary)
Purification (Commentary)
Organism
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli and purified. Wild-type and active site mutants
Thermotoga maritima
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-glutamine + H2O
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
L-glutamate + NH3
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Thermotoga maritima
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
0.8
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Thermotoga maritima
Cloned(Commentary) (protein specific)
Commentary
Organism
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli
Thermotoga maritima
Engineering (protein specific)
Protein Variants
Commentary
Organism
C9A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
D11N
mutation in subunit HisF. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
Thermotoga maritima
D130N
the kcat value is reduced by a factor of about 400-500, and the Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is increased almost 20fold. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
Thermotoga maritima
D176N
mutation in subunit HisF. The variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
Thermotoga maritima
D183N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
D51N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
K19S
mutation in subunit HisF. The ammonia-dependent reactions of isolated subunit HisF_K19S is similarly efficient as that of wild-type HisF. The efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired
Thermotoga maritima
additional information
eight conserved amino acids at the putative active site of subunit HisF are exchanged by site-directed mutagenesis, and the purified variants are investigated by steady state kinetics. Aspartate 11 appears to be essential for the synthase activity both in vitro and in vivo, and aspartate 130 can be partially replaced only by glutamate
Thermotoga maritima
N103A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
0.32
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
Purification (Commentary) (protein specific)
Commentary
Organism
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli and purified. Wild-type and active site mutants
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-glutamine + H2O
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
L-glutamate + NH3
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
748148
Thermotoga maritima DSM 3109
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Thermotoga maritima
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
0.8
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Thermotoga maritima
General Information
General Information
Commentary
Organism
metabolism
the enzyme links histidine and de novo purine biosynthesis
Thermotoga maritima
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme links histidine and de novo purine biosynthesis
Thermotoga maritima
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0006
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
1.4
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0006
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25C
Thermotoga maritima
1.4
-
L-glutamine
pH 8.5, 25C
Thermotoga maritima
Other publictions for EC 4.3.1.B2
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
Synonyms
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)
728756
Liebold
The interaction of ammonia and ...
Thermotoga maritima
Protein Sci.
19
1774-1782
2010
-
-
1
-
1
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
726941
Myers
Reaction coupling through inte ...
Saccharomyces cerevisiae
Biochemistry
44
11974-11985
2005
-
-
-
-
5
-
-
18
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
1
-
-
18
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
18
18
727051
Demin
Kinetic model of imidazologlyc ...
Escherichia coli
Biochemistry
69
1324-1335
2004
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
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-
-
-
-
-
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-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
726938
Chaudhuri
Toward understanding the mecha ...
Saccharomyces cerevisiae
Biochemistry
42
7003-7012
2003
-
-
-
1
-
-
2
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
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-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726939
Myers
Substrate-induced changes in t ...
Saccharomyces cerevisiae
Biochemistry
42
7013-7022
2003
-
-
-
-
7
-
3
22
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
1
1
-
-
22
1
-
-
-
7
-
-
-
-
-
-
-
7
-
-
3
7
22
-
-
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
22
1
-
-
-
-
-
-
-
24
24
727791
Omi
Structure of imidazole glycero ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biochem.
132
759-765
2002
-
-
-
1
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-
-
-
-
-
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2
-
92
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
728807
Douangamath
Structural evidence for ammoni ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Structure
10
185-193
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
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7