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

BRENDA support

Literature summary for 2.7.1.226 extracted from

  • Nagata, R.; Fujihashi, M.; Kawamura, H.; Sato, T.; Fujita, T.; Atomi, H.; Miki, K.
    Structural study on the reaction mechanism of a free serine kinase involved in cysteine biosynthesis (2017), ACS Chem. Biol., 12, 1514-1523 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Thermococcus kodakarensis

Crystallization (Commentary)

Crystallization (Comment) Organism
the overall structure is divided into two domains , with a large cleft in the AMP complex and in the ADP complex. The cleft is closed in the ternary product complex with O-phospho-L-serine and AMP. The closure may reorient the carboxyl group of E30 near to the Ogamma atom of Ser. The Ogamma atom may be deprotonated by E30 and attack the beta-phosphate of ADP to form O-phospho-L-serine Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
E30A substantial decrease in the activity Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + L-serine Thermococcus kodakarensis
-
AMP + O-phospho-L-serine
-
?
ADP + L-serine Thermococcus kodakarensis ATCC BAA-918
-
AMP + O-phospho-L-serine
-
?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JD03
-
-
Thermococcus kodakarensis ATCC BAA-918 Q5JD03
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + L-serine
-
Thermococcus kodakarensis AMP + O-phospho-L-serine
-
?
ADP + L-serine
-
Thermococcus kodakarensis ATCC BAA-918 AMP + O-phospho-L-serine
-
?

Synonyms

Synonyms Comment Organism
serK
-
Thermococcus kodakarensis

General Information

General Information Comment Organism
physiological function SerK is a free serine kinase involved in cysteine biosynthesis Thermococcus kodakarensis