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

BRENDA support

Literature summary for 2.4.1.248 extracted from

  • Ichinose, H.; Suzuki, R.; Miyazaki, T.; Kimura, K.; Momma, M.; Suzuki, N.; Fujimoto, Z.; Kimura, A.; Funane, K.
    Paenibacillus sp. 598K 6-alpha-glucosyltransferase is essential for cycloisomaltooligosaccharide synthesis from alpha-(1->4)-glucan (2017), Appl. Microbiol. Biotechnol., 101, 4115-4128 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Paenibacillus sp. 598K

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch Paenibacillus sp. 598K key enzyme to synthesize alpha-(1->6)-glucan for cycloisomaltooligosaccharide production in dextran-free environments ?
-
?

Organism

Organism UniProt Comment Textmining
Paenibacillus sp. 598K G9MBW2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Paenibacillus sp. 598K

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme displays extremely low activity against 4-nitrophenyl alpha-glucopyranoside. It does not display any hydrolytic activity against 4-nitrophenyl alpha-mannopyranoside, 4-nitrophenyl alpha-galactopyranoside, and 4-nitrophenyl alpha-xylopyranoside Paenibacillus sp. 598K ?
-
-
starch key enzyme to synthesize alpha-(1->6)-glucan for cycloisomaltooligosaccharide production in dextran-free environments Paenibacillus sp. 598K ?
-
?
starch the enzyme has a strong alpha-(1->4) to alpha-(1->6) transglucosylation activity. The enzyme exhibits higher hydrolysis activity against alpha-(1->4)-linked glucan than against alpha-(1->6)-linked glucan. It elongates alpha-(1->6)-linked glucooligosaccharide to at least a degree of polymerization of 10 through a successive transglucosylation reaction Paenibacillus sp. 598K cycloisomaltooligosaccharide
-
?

Synonyms

Synonyms Comment Organism
cit
-
Paenibacillus sp. 598K