Literature summary for 2.6.1.9 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.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WML7	-	-
Mycobacterium tuberculosis H37Rv	P9WML7	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

kcat/KM [mM/s]

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