Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.165 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)

Cloned (Comment) Organism
expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X1S1
-
-
Thermotoga maritima DSM 3109 Q9X1S1
-
-

Synonyms

Synonyms Comment Organism
TM1585
-
Thermotoga maritima

pI Value

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

General Information

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