Literature summary for 4.6.1.17 extracted from

Kanaujia, S.P.; Jeyakanthan, J.; Nakagawa, N.; Balasubramaniam, S.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8 (2010), Acta Crystallogr. Sect. D, 66, 821-833.

Search for more literature for 4.6.1.17

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
GTP-bound crystal structure	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermus thermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC	Thermus thermophilus	?	-	?
additional information	the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	?	-	?

Subunits

Subunits	Comment	Organism
hexamer	-	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
MoaC	the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC	Thermus thermophilus

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Release 2023.1 (January 2023)