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Literature summary extracted from

  • Schwarzenbacher, R.; McMullan, D.; Krishna, S.; Xu, Q.; Miller, M.; Canaves, J.; Elsliger, M.; Floyd, R.; Grzechnik, S.; Jaroszewski, L.; Klock, H.; Koesema, E.; Kovarik, J.; Kreusch, A.; Kuhn, P.; McPhillips, T.; Morse, A.; Quijano, K.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
    Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 A resolution reveals a new fold (2006), Proteins, 65, 243-248 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.165 expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.165 the crystal structure is determined to a nominal resolution of 2.70 A Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.165 44589
-
calculated from sequence Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.165 Thermotoga maritima Q9X1S1
-
-
2.7.1.165 Thermotoga maritima DSM 3109 Q9X1S1
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.1.165 TM1585
-
Thermotoga maritima

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.165 Thermotoga maritima calculated from sequence
-
5.73

General Information

EC Number General Information Comment Organism
2.7.1.165 metabolism the enzyme is part of the Entner-Doudoroff pathway II (non-phosphorylative) Thermotoga maritima