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Literature summary for 2.6.1.9 extracted from

  • Fernandez, F.J.; Vega, M.C.; Lehmann, F.; Sandmeier, E.; Gehring, H.; Christen, P.; Wilmanns, M.
    Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase (2004), J. Biol. Chem., 279, 21478-21488.
    View publication on PubMed
Search for more literature for 2.6.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3) and B834(DE3), respectively Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and selenomethionine-labeled enzyme, with or without bound pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, sitting drop vapour diffusion method, 0.001 ml equal volumes of protein and reservoir solutions, 20°C, 50% v/v ethylene glycol, 5% w/v PEG 1000, sodium acetate, pH 5.1, 2-3 weeks, X-ray diffraction structure determination and analysis at 3.5 A resolution Thermotoga maritima

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.8
-
 L-histidinol phosphate pH 8.0, 20°C Thermotoga maritima
2.3
-
 L-tyrosine pH 8.0, 20°C Thermotoga maritima
3.4
-
 L-tryptophan pH 8.0, 20°C Thermotoga maritima
38
-
 L-phenylalanine pH 8.0, 20°C Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-histidinol phosphate + 2-oxoglutarate Thermotoga maritima catalytic reaction pathway, histidine biosynthesis 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
 r
additional information Thermotoga maritima enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X0D0 gene tmHspAT
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) and B834(DE3), respectively Thermotoga maritima

Reaction

Reaction Comment Organism Reaction ID
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate mechanism via gem-diamino, aldimine, and ketimine reaction intermediates, active site structure analysis, overview Thermotoga maritima
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidinol phosphate + 2-oxoglutarate
-
 Thermotoga maritima 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
 r
L-histidinol phosphate + 2-oxoglutarate catalytic reaction pathway, histidine biosynthesis Thermotoga maritima 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
 r
L-phenylalanine + 2-oxoglutarate low activity with Thermotoga maritima phenylpyruvate + L-glutamate
-
 r
L-tryptophan + 2-oxoglutarate
-
 Thermotoga maritima 3-indole-2-oxopropanoate + L-glutamate
-
 r
L-tyrosine + 2-oxoglutarate
-
 Thermotoga maritima 3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
 r
additional information enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo Thermotoga maritima ?
-
 ?
additional information no activity with L-histidine Thermotoga maritima ?
-
 ?

Synonyms

Synonyms Comment Organism
histidinol-phosphate aminotransferase
-
 Thermotoga maritima
HspAT
-
 Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 above Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.009
-
 L-phenylalanine pH 8.0, 25°C Thermotoga maritima
0.014
-
 L-tryptophan pH 8.0, 25°C Thermotoga maritima
0.043
-
 L-tyrosine pH 8.0, 25°C Thermotoga maritima
0.046
-
 L-histidinol phosphate pH 8.0, 25°C Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermotoga maritima

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate covalently bound Thermotoga maritima