Literature summary for 2.1.1.107 extracted from

Vevodova, J.; Graham, R.M.; Raux, E.; Schubert, H.L.; Roper, D.I.; Brindley, A.A.; Ian Scott, A.; Roessner, C.A.; Stamford, N.P.; Elizabeth Stroupe, M.; Getzoff, E.D.; Warren, M.J.; Wilson, K.S.
Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis (2004), J. Mol. Biol., 344, 419-433.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme topology diagramm	Pseudomonas denitrificans (nom. rej.)

Protein Variants

Protein Variants	Comment	Organism
D47N	binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1	Pseudomonas denitrificans (nom. rej.)
F106A	considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity	Pseudomonas denitrificans (nom. rej.)
L49A	binds about half the quantity of S-adenosyl-L-methionine compared with wild-type, reaction products are oxidised forms of both precorrin-1 and precorrin-2	Pseudomonas denitrificans (nom. rej.)
M184A	slight enzymic activity	Pseudomonas denitrificans (nom. rej.)
T130A	considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine	Pseudomonas denitrificans (nom. rej.)
Y183A	considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity	Pseudomonas denitrificans (nom. rej.)

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas denitrificans (nom. rej.)	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Pseudomonas denitrificans (nom. rej.)

Synonyms

Synonyms	Comment	Organism
SUMT	-	Pseudomonas denitrificans (nom. rej.)

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Release 2023.1 (January 2023)