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Literature summary for 4.4.1.13 extracted from

  • Oogai, S.; Fukuta, M.; Watanabe, K.; Inafuku, M.; Oku, H.
    Molecular characterization of mimosinase and cystathionine beta-lyase in the Mimosoideae subfamily member Mimosa pudica (2019), J. Plant Res., 132, 667-680 .
    View publication on PubMed
Search for more literature for 4.4.1.13

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3) Mimosa pudica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4
-
 cystathionine pH 8.5, 37°C, recombinant enzyme Mimosa pudica

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme sequence contains a signal peptide Mimosa pudica
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cystathionine + H2O Mimosa pudica
-
 homocysteine + pyruvate + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Mimosa pudica A0A0M3VI47
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Mimosa pudica
-
seedling
-
 Mimosa pudica
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cystathionine + H2O
-
 Mimosa pudica homocysteine + pyruvate + NH3
-
 ?
additional information substrate docking study. The largest attractive force that stabilizes the amino group of the ethyl chain moiety is contributed by Arg433. The negative charge of the carboxyl group in the ethyl chain is balanced by a hydrogen bond between it and amino group of Lys271. The propyl chain moiety of cystathionine is stabilized by the guanidium groups of two residues, Arg179 and Arg122'. Phosphate group of PLP forms two hydrogen bonds between hydroxy hydrogen of Ser268 and guanidium hydrogen of Arg122' Mimosa pudica ?
-
 ?

Synonyms

Synonyms Comment Organism
CBL
-
 Mimosa pudica
Mp CBL
-
 Mimosa pudica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Mimosa pudica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 purified recombinant GST-tagged enzyme, pH 8.0, stable up to Mimosa pudica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21000
-
 cystathionine pH 8.5, 37°C, recombinant enzyme Mimosa pudica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Mimosa pudica

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Mimosa pudica

General Information

General Information Comment Organism
metabolism molecular relationship between cystathionine beta-lyase and mimosinase (UniProt ID U6BYK3, EC 3.5.1.61). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate Mimosa pudica
additional information homology modeling and molecular dynamics simulations of Mp CBL. Active site structure Mimosa pudica

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8750
-
 cystathionine pH 8.5, 37°C, recombinant enzyme Mimosa pudica