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Literature summary for 3.4.21.B30 extracted from

  • Lee, M.H.; Ohta, T.; Walker, G.C.
    A monocysteine approach for probing the structure and interactions of the UmuD protein (1994), J. Bacteriol., 176, 4825-4837.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B30

Protein Variants

Protein Variants Comment Organism
A89C reduced ability to for a heterodimer with UmuD' Escherichia coli
C24A ability to participate in UV mutagenesis and RecA-mediated cleavage are similar to that of the wild-type enzyme Escherichia coli
D126C reduced ability to form a homodimer and a heterodimer with UmuD' Escherichia coli
L44C reduced ability to form a homodimer Escherichia coli
S57C reduced activity in UV mutagenesis Escherichia coli
S60C similar in iodoacetate reactivity but cross-links less efficiently by I2 oxidation than the wild-type enzyme, reduced activity in UV mutagenesis Escherichia coli
S67C only 9% as active as the wild-type enzyme in UV mutagenesis Escherichia coli
V34C reduced activity in UV mutagenesis Escherichia coli

General Stability

General Stability Organism
UmuD/UmuD' heterodimer is more stable than each of the homodimers Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli role in UV mutagenesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity, wild-type and mutants Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information role in UV mutagenesis Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer enzyme can form homodimers, crosslinking experiments, SDS-PAGE Escherichia coli