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

BRENDA support

Literature summary for 2.7.7.65 extracted from

  • Vorobiev, S.M.; Neely, H.; Yu, B.; Seetharaman, J.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Hunt, J.F.
    Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product (2012), J. Struct. Funct. Genomics, 13, 177-183.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of G-A1U3W3 (residues 155-312) is determined at 1.83 A resolution using the selenomethionyl SAD method. Co-crystallization with GTP results in enzymatic synthesis of c-di-GMP Marinobacter nauticus

Protein Variants

Protein Variants Comment Organism
additional information isolated G-A1U3W3 domain (residues 155–312) has full enzymatic activity and synthesize c-di-GMP Marinobacter nauticus

Organism

Organism UniProt Comment Textmining
Marinobacter nauticus A1U3W3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
-
Marinobacter nauticus cyclic di-3',5'-guanylate + diphosphate
-
?

Synonyms

Synonyms Comment Organism
GG(D/E)EF diguanylate cyclase
-
Marinobacter nauticus