Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Burton, R.L.; Chen, S.; Xu, X.L.; Grant, G.A.
    A novel mechanism for substrate inhibition in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase (2007), J. Biol. Chem., 282, 31517-31524.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.95 H447A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.16, kcat: 1446, Ki (mM) (3-phosphohydroxypyruvate): 0.87, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type Mycobacterium tuberculosis
1.1.1.95 K439A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.075, kcat: 368, Ki (mM) (3-phosphohydroxypyruvate): 0.054, mutant displays partial uncompetitive substrate inhibition, mutant retains dual pH optima Mycobacterium tuberculosis
1.1.1.95 R446A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.123 kcat: 467, Ki (mM) (3-phosphohydroxypyruvate): 0.289, mutant displays partial uncompetitive substrate inhibition, no dual pH optima compared to wild-type Mycobacterium tuberculosis
1.1.1.95 R451A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.19, kcat: 1881, Ki (mM) (3-phosphohydroxypyruvate): 0.95, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type Mycobacterium tuberculosis
1.1.1.95 R501A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.18, kcat: 1989, Ki (mM) (3-phosphohydroxypyruvate): 1.02, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type Mycobacterium tuberculosis
1.1.1.95 R501A/R451A/K439A anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.243, kcat: 1558, Ki (mM) (3-phosphohydroxypyruvate): 7.218, mutant displays only little uncompetitive substrate inhibition, no dual pH optima compared to wild-type Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.95 3-phosphohydroxypyruvate uncompetitive substrate inhibition at high substrate concentration Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.95 0.075
-
 3-phosphohydroxypyruvate mutant K439A Mycobacterium tuberculosis
1.1.1.95 0.123
-
 3-phosphohydroxypyruvate mutant R446A Mycobacterium tuberculosis
1.1.1.95 0.16
-
 3-phosphohydroxypyruvate mutant H447A Mycobacterium tuberculosis
1.1.1.95 0.17
-
 3-phosphohydroxypyruvate
-
 Mycobacterium tuberculosis
1.1.1.95 0.18
-
 3-phosphohydroxypyruvate mutant R501A Mycobacterium tuberculosis
1.1.1.95 0.19
-
 3-phosphohydroxypyruvate mutant R451A Mycobacterium tuberculosis
1.1.1.95 0.243
-
 3-phosphohydroxypyruvate mutant R501A/R451A/K439A Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Mycobacterium tuberculosis P9WNX3
-
-
1.1.1.95 Mycobacterium tuberculosis H37Rv P9WNX3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 3-phosphohydroxypyruvate + NAD+
-
 Mycobacterium tuberculosis ?
-
 r
1.1.1.95 3-phosphohydroxypyruvate + NAD+
-
 Mycobacterium tuberculosis H37Rv ?
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.95 3-phosphoglycerate dehydrogenase
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.95 368
-
 3-phosphohydroxypyruvate mutant K439A Mycobacterium tuberculosis
1.1.1.95 467
-
 3-phosphohydroxypyruvate mutant R446A Mycobacterium tuberculosis
1.1.1.95 1446
-
 3-phosphohydroxypyruvate mutant H447A Mycobacterium tuberculosis
1.1.1.95 1558
-
 3-phosphohydroxypyruvate mutant R501A/R451A/K439A Mycobacterium tuberculosis
1.1.1.95 1881
-
 3-phosphohydroxypyruvate mutant R451A Mycobacterium tuberculosis
1.1.1.95 1989
-
 3-phosphohydroxypyruvate mutant R501A Mycobacterium tuberculosis
1.1.1.95 2461
-
 3-phosphohydroxypyruvate
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.95 5.2
-
 enzyme possess a dual pH optimum. A significant decrease in the Ki for substrate inhibition at pH values corresponding to the valley between these optima is responsible for this phenomenon Mycobacterium tuberculosis
1.1.1.95 8
-
 enzyme possess a dual pH optimum. A significant decrease in the Ki for substrate inhibition at pH values corresponding to the valley between these optima is responsible for this phenomenon Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.95 5.2 5.7 at approximately pH 5.7 the activity starts increasing again and reaches a new optimum at approximately pH 5.2 before decreasing once again Mycobacterium tuberculosis
1.1.1.95 7.5 9.5 activity is relatively constant between pH 7.5-9.5. Above pH 9.5 and below pH 7.5 activity falls off rapidly Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.95 0.054
-
 3-phosphohydroxypyruvate mutant K439A Mycobacterium tuberculosis
1.1.1.95 0.289
-
 3-phosphohydroxypyruvate mutant R446A Mycobacterium tuberculosis
1.1.1.95 0.87
-
 3-phosphohydroxypyruvate mutant H447A Mycobacterium tuberculosis
1.1.1.95 0.95
-
 3-phosphohydroxypyruvate
-
 Mycobacterium tuberculosis
1.1.1.95 0.95
-
 3-phosphohydroxypyruvate mutant R451A Mycobacterium tuberculosis
1.1.1.95 1.02
-
 3-phosphohydroxypyruvate mutant R501A Mycobacterium tuberculosis
1.1.1.95 7.218
-
 3-phosphohydroxypyruvate mutant R501A/R451A/K439A Mycobacterium tuberculosis