Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-90 |
Sentence |
denotes |
Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli. |
T2 |
91-306 |
Sentence |
denotes |
GTP cyclohydrolase I, an enzyme that catalyzes the first reaction in the pathway for the biosynthesis of the pteridine portion of folic acid, was purified from Escherichia coli by 3,900-fold to apparent homogeneity. |
T3 |
307-352 |
Sentence |
denotes |
Its molecular weight is estimated at 210,000. |
T4 |
353-503 |
Sentence |
denotes |
At relatively high concentrations of salt (e.g. 0.3 M KCl) the enzyme can be dissociated into seemingly identical subunits of 51,000 molecular weight. |
T5 |
504-545 |
Sentence |
denotes |
Removal of the salt allows reassociation. |
T6 |
546-723 |
Sentence |
denotes |
GTP, ATP, and inorganic orthophosphate at concentration of 5 muM, 100muM, and 0.2 mM, respectively, promote the reassociation of the subunits even in the presence of 0.3 M salt. |
T7 |
724-774 |
Sentence |
denotes |
The subunits have little or no catalytic activity. |
T8 |
775-998 |
Sentence |
denotes |
When the enzyme was subjected to electrophoresis on polyacrylamide gel under denaturing conditions (in the presence of sodium dodecyl sulfate) only one protein band was evident; its molecular weight was estimated at 25,500. |
T9 |
999-1080 |
Sentence |
denotes |
Proline was determined as the only NH2-terminal amino acid residue of the enzyme. |
T10 |
1081-1224 |
Sentence |
denotes |
These observations suggest that the enzyme consists of four identical subunits and that each subunit contains two identical polypeptide chains. |
T11 |
1225-1323 |
Sentence |
denotes |
Enough GTP was bound to the enzyme to suggest that each polypeptide contains one GTP binding site. |
T12 |
1324-1357 |
Sentence |
denotes |
The Km value for GTP IS 0.02 MuM. |
T13 |
1358-1493 |
Sentence |
denotes |
ATP, dGTP, and guanosine 5'-tetraphosphate are competitive inhibitors with Ki values of 0.25 muM, 0.24 muM, and 0.13 muM, respectively. |
T14 |
1494-1539 |
Sentence |
denotes |
Orthophosphate is an uncompetitive inhibitor. |
T15 |
1540-1615 |
Sentence |
denotes |
The enzyme is relatively heat-stable; its half-life at 82 degrees is 7 min. |
T16 |
1616-1705 |
Sentence |
denotes |
Salt (NaCl, KCl, NH4Cl) at a concentration of 0.1 M activates the enzyme by 4- to 5-fold. |
T17 |
1706-1889 |
Sentence |
denotes |
The only products of the action of the enzyme are formate and the triphosphoester of 2-amino-4-hydroxy-6-(D-erythro-1',2',3'-trihydroxypropyl)-7,8-dihydropteridine (H2-neopterin-PPP). |
T18 |
1890-2033 |
Sentence |
denotes |
The evidence strongly suggests that this single enzyme catalyzes 4 independent chemical reactions in the conversion of GTP to H2-neopterin-PPP. |
T1 |
0-90 |
Sentence |
denotes |
Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli. |
T2 |
91-306 |
Sentence |
denotes |
GTP cyclohydrolase I, an enzyme that catalyzes the first reaction in the pathway for the biosynthesis of the pteridine portion of folic acid, was purified from Escherichia coli by 3,900-fold to apparent homogeneity. |
T3 |
307-352 |
Sentence |
denotes |
Its molecular weight is estimated at 210,000. |
T4 |
353-503 |
Sentence |
denotes |
At relatively high concentrations of salt (e.g. 0.3 M KCl) the enzyme can be dissociated into seemingly identical subunits of 51,000 molecular weight. |
T5 |
504-545 |
Sentence |
denotes |
Removal of the salt allows reassociation. |
T6 |
546-723 |
Sentence |
denotes |
GTP, ATP, and inorganic orthophosphate at concentration of 5 muM, 100muM, and 0.2 mM, respectively, promote the reassociation of the subunits even in the presence of 0.3 M salt. |
T7 |
724-774 |
Sentence |
denotes |
The subunits have little or no catalytic activity. |
T8 |
775-998 |
Sentence |
denotes |
When the enzyme was subjected to electrophoresis on polyacrylamide gel under denaturing conditions (in the presence of sodium dodecyl sulfate) only one protein band was evident; its molecular weight was estimated at 25,500. |
T9 |
999-1080 |
Sentence |
denotes |
Proline was determined as the only NH2-terminal amino acid residue of the enzyme. |
T10 |
1081-1224 |
Sentence |
denotes |
These observations suggest that the enzyme consists of four identical subunits and that each subunit contains two identical polypeptide chains. |
T11 |
1225-1323 |
Sentence |
denotes |
Enough GTP was bound to the enzyme to suggest that each polypeptide contains one GTP binding site. |
T12 |
1324-1357 |
Sentence |
denotes |
The Km value for GTP IS 0.02 MuM. |
T13 |
1358-1493 |
Sentence |
denotes |
ATP, dGTP, and guanosine 5'-tetraphosphate are competitive inhibitors with Ki values of 0.25 muM, 0.24 muM, and 0.13 muM, respectively. |
T14 |
1494-1539 |
Sentence |
denotes |
Orthophosphate is an uncompetitive inhibitor. |
T15 |
1540-1615 |
Sentence |
denotes |
The enzyme is relatively heat-stable; its half-life at 82 degrees is 7 min. |
T16 |
1616-1705 |
Sentence |
denotes |
Salt (NaCl, KCl, NH4Cl) at a concentration of 0.1 M activates the enzyme by 4- to 5-fold. |
T17 |
1706-1889 |
Sentence |
denotes |
The only products of the action of the enzyme are formate and the triphosphoester of 2-amino-4-hydroxy-6-(D-erythro-1',2',3'-trihydroxypropyl)-7,8-dihydropteridine (H2-neopterin-PPP). |
T18 |
1890-2033 |
Sentence |
denotes |
The evidence strongly suggests that this single enzyme catalyzes 4 independent chemical reactions in the conversion of GTP to H2-neopterin-PPP. |