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Literature summary for 4.2.2.12 extracted from

  • Maruyama, Y.; Hashimoto, W.; Mikami, B.; Murata, K.
    Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism (2005), J. Mol. Biol., 350, 974-986.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus sp. (in: Bacteria)

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion, resolution of N194A/PyrMan, N194/pentasacharide and ligand-free form are 1.8, 2.1 and 2.3 respectively Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
H246A mutant with 2fold decreased Km for xanthan, 500fold decreased turnover number Bacillus sp. (in: Bacteria)
N194A mutant with 2fold decreased Km for xanthan, 570fold decreased turnover number Bacillus sp. (in: Bacteria)
Y255F mutant with 2fold decreased Km for xanthan, 360fold decreased turnover number Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
Xanthan 0.25 mg/ml, wild-type Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) GL1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xanthan
-
Bacillus sp. (in: Bacteria) pyruvylate mannose + oligosaccharide
-
?
xanthan
-
Bacillus sp. (in: Bacteria) GL1 pyruvylate mannose + oligosaccharide
-
?

Synonyms

Synonyms Comment Organism
xanthan lyase
-
Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2170
-
Xanthan wild-type Bacillus sp. (in: Bacteria)