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Literature summary for 3.1.21.4 extracted from

  • Callahan, S.J.; Luyten, Y.A.; Gupta, Y.K.; Wilson, G.G.; Roberts, R.J.; Morgan, R.D.; Aggarwal, A.K.
    Structure of type IIL restriction-modification enzyme MmeI in complex with DNA has implications for engineering new specificities (2016), PLoS Biol., 14, e1002471 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of MmeI in complex with its DNA substrate (a 29-mer DNA duplex containing a single MmeI recognition site (TCCGAC)) and an S-adenosylmethionine analog sinefungin. The co-crystals are obtained in the presence of sinefungin and diffracted to 2.6 A resolution with synchrotron radiation. They belong to space group P1 with unit cell dimensions of a = 61.87 A, b = 95.29 A, c = 161.96 A, alpha = 72.84°, beta = 89.15°, and gamma = 71.61°, and contain two MmeI/DNA/sinefungin complexes in the crystallographic asymmetric unit Methylophilus methylotrophus

Inhibitors

Inhibitors Comment Organism Structure
sinefungin
-
Methylophilus methylotrophus

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus B2MU09
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methylophilus methylotrophus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O the enzyme is resilient to specificity changes at the first position of the recognition sequence (5'-TCCRAC-3') Methylophilus methylotrophus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Methylophilus methylotrophus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
assay at Methylophilus methylotrophus