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Literature summary extracted from

  • Nasir, N.; Anant, A.; Vyas, R.; Biswal, B.K.
    Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities (2016), Sci. Rep., 6, 18880.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.9
-
Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.9 hydrophilic residues in the substrate binding pocket and N-terminal lid allow the entry and binding of its preferential substrate. The pyridoxal phosphate cofactor binds as an internal aldimine via a Schiff ’s base with epsilon-N of Lys232. The inhibitor 2-(N-morpholino)ethanesulfonic acid binds in the active site. The N-terminal lid is restructured upon binding of ligand, leading to a closed conformation of the enzyme necessary for the binding and probable catalysis of the substrate. The closing of the lid upon ligand binding causes Tyr25 to sweep into the active site region and interact with the ligand Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.9 Y127F about 20% of wild-type activity with L-histidinol phosphate, no significant loss of activity with phenylalanine Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.9 2-(N-morpholino)ethanesulfonic acid specific inhibitor Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.9 0.42
-
L-histidinol phosphate pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 7.1
-
L-phenylalanine pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 9.8
-
L-tyrosine pH 8.4, 37°C Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.9 Mycobacterium tuberculosis P9WML7
-
-
2.6.1.9 Mycobacterium tuberculosis H37Rv P9WML7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.9 L-histidinol phosphate + 2-oxoglutarate
-
Mycobacterium tuberculosis 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Glu
-
?
2.6.1.9 L-histidinol phosphate + 2-oxoglutarate
-
Mycobacterium tuberculosis H37Rv 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Glu
-
?
2.6.1.9 L-phenylalanine + 2-oxoglutarate
-
Mycobacterium tuberculosis phenylpyruvate + L-glutamate
-
?
2.6.1.9 L-phenylalanine + 2-oxoglutarate
-
Mycobacterium tuberculosis H37Rv phenylpyruvate + L-glutamate
-
?
2.6.1.9 L-tyrosine + 2-oxoglutarate
-
Mycobacterium tuberculosis 3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
-
?
2.6.1.9 L-tyrosine + 2-oxoglutarate
-
Mycobacterium tuberculosis H37Rv 3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.9 220
-
L-phenylalanine pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 426
-
L-histidinol phosphate pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 3100
-
L-tyrosine pH 8.4, 37°C Mycobacterium tuberculosis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.9 30
-
L-phenylalanine pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 320
-
L-tyrosine pH 8.4, 37°C Mycobacterium tuberculosis
2.6.1.9 1020
-
L-histidinol phosphate pH 8.4, 37°C Mycobacterium tuberculosis