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Literature summary for 1.2.1.88 extracted from

  • Campbell, A.C.; Bogner, A.N.; Mao, Y.; Becker, D.F.; Tanner, J.J.
    Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-gamma-semialdehyde dehydrogenase active site of bifunctional proline utilization A (2021), Arch. Biochem. Biophys., 698, 108727 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Sinorhizobium meliloti

Crystallization (Commentary)

Crystallization (Comment) Organism
PutA with the following ligands bound in the GSALDH active site: NADH, D-proline, trans-4-hydroxy-D-proline, cis-4-hydroxy-D-proline, L-proline, and trans-4-hydroxy-L-proline, sitting drop vapor diffusion method, using 19% (w/v) PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate Sinorhizobium meliloti

Inhibitors

Inhibitors Comment Organism Structure
cis-4-hydroxy-D-proline weak inhibitor Sinorhizobium meliloti
D-proline weak inhibitor Sinorhizobium meliloti
L-proline weak inhibitor Sinorhizobium meliloti
additional information cis-4-hydroxy-L-proline does not inhibit the enzyme activity Sinorhizobium meliloti
trans-4-hydroxy-D-proline weak inhibitor Sinorhizobium meliloti
trans-4-hydroxy-L-proline weak inhibitor Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate 5-semialdehyde + NAD+ + H2O Sinorhizobium meliloti
-
 L-glutamate + NADH + H+
-
 ir
L-glutamate 5-semialdehyde + NAD+ + H2O Sinorhizobium meliloti SM11
-
 L-glutamate + NADH + H+
-
 ir

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti F7X6I3
-
-
Sinorhizobium meliloti SM11 F7X6I3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate 5-semialdehyde + NAD+ + H2O
-
 Sinorhizobium meliloti L-glutamate + NADH + H+
-
 ir
L-glutamate 5-semialdehyde + NAD+ + H2O
-
 Sinorhizobium meliloti SM11 L-glutamate + NADH + H+
-
 ir

Synonyms

Synonyms Comment Organism
Aldh4a1
-
 Sinorhizobium meliloti
GSAL dehydrogenase
-
 Sinorhizobium meliloti
GSALDH
-
 Sinorhizobium meliloti
l-glutamate-gamma-semialdehyde dehydrogenase
-
 Sinorhizobium meliloti
PutA proline utilization A protein, bifunctional proline catabolic enzyme that catalyzes the 4-electron oxidation of L-proline to L-glutamate using spatially-separated proline dehydrogenase and L-glutamate-gamma-semialdehyde dehydrogenase active sites Sinorhizobium meliloti

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Sinorhizobium meliloti

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5
-
 D-proline competitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
2 5 cis-4-hydroxy-D-proline mixed-type inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
4.5
-
 trans-4-hydroxy-D-proline competitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
4.5
-
 D-proline uncompetitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
7
-
 trans-4-hydroxy-L-proline competitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
8
-
 cis-4-hydroxy-D-proline competitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
10
-
 trans-4-hydroxy-D-proline mixed-type inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
11
-
 L-proline competitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
19
-
 L-proline uncompetitive inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti
27
-
 trans-4-hydroxy-L-proline mixed-type inhibition model, at pH 7.5, temperature not specified in the publication Sinorhizobium meliloti