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Literature summary for 4.2.2.11 extracted from

  • Matsubara, Y.; Iwasaki, K.I.; Muramatsu, T.
    Action of poly(alpha-L-guluronate) lyase from Corynebacterium sp. ALY-1 strain on saturated oligoguluronates (1998), Biosci. Biotechnol. Biochem., 62, 1055-1060.
    View publication on PubMed
Search for more literature for 4.2.2.11

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.077
-
 saturated deca((1-4)-alpha-L-guluronan) pH 7.0, 50 mM phosphate buffer Corynebacterium sp.
0.099
-
 saturated hepta((1-4)-alpha-L-guluronan) pH 7.0, 50 mM phosphate buffer Corynebacterium sp.
0.11
-
 saturated hexa((1-4)-alpha-L-guluronan) pH 7.0, 50 mM phosphate buffer Corynebacterium sp.
0.3
-
 saturated penta((1-4)-alpha-L-guluronan) pH 7.0, 50 mM phosphate buffer Corynebacterium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Corynebacterium sp.
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
poly-alpha-L-guluronic acid Corynebacterium sp.
-
 unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
 ALY-1 strain
-
Corynebacterium sp. ALY-1
-
 ALY-1 strain
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly-alpha-L-guluronic acid
-
 Corynebacterium sp. ?
-
 ?
poly-alpha-L-guluronic acid
-
 Corynebacterium sp. ALY-1 ?
-
 ?
poly-alpha-L-guluronic acid
-
 Corynebacterium sp. unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
 ?
saturated deca((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ?
-
 ?
saturated deca((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ALY-1 ?
-
 ?
saturated hepta((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ?
-
 ?
saturated hepta((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ALY-1 ?
-
 ?
saturated hexa((1-4)-alpha-L-guluronan) rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end Corynebacterium sp. unsaturated tetramer and a saturated dimer main products, the catalytic site is matched to the linkage between the second and the third uronic residue from the non-reducing end, the degradation of tri((1-4)-alpha-L-guluronan) does not apparently occur ?
saturated hexa((1-4)-alpha-L-guluronan) rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end Corynebacterium sp. ALY-1 unsaturated tetramer and a saturated dimer main products, the catalytic site is matched to the linkage between the second and the third uronic residue from the non-reducing end, the degradation of tri((1-4)-alpha-L-guluronan) does not apparently occur ?
saturated penta((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((1-4)-alpha-L-guluronan)
-
 ?
saturated tetra((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ?
-
 ?
saturated tetra((1-4)-alpha-L-guluronan)
-
 Corynebacterium sp. ALY-1 ?
-
 ?