Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.2.4 extracted from

  • Bujara, M.; Schuemperli, M.; Billerbeck, S.; Heinemann, M.; Panke, S.
    Exploiting cell-free systems: Implementation and debugging of a system of biotransformations (2010), Biotechnol. Bioeng., 106, 376-389.
    View publication on PubMed
Search for more literature for 3.2.2.4

Protein Variants

Protein Variants Comment Organism
additional information AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene amn
-
Escherichia coli W3110 / ATCC 27325
-
 gene amn
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview Escherichia coli ?
-
 ?
additional information AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview Escherichia coli W3110 / ATCC 27325 ?
-
 ?