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Literature summary for 4.2.2.11 extracted from

  • Matsubara, Y.; Kawada, R.; Iwasaki, K.; Oda, T.; Muramatsu, T.
    Extracellular poly(alpha-L-guluronate)lyase from Corynebacterium sp.: purification, characteristics, and conformational properties (1998), J. Protein Chem., 17, 29-36.
    View publication on PubMed
Search for more literature for 4.2.2.11

Inhibitors

Inhibitors Comment Organism Structure
CuCl2 1 mM, 58% remaining activity Corynebacterium sp.
EDTA 1 mM concentration causes 83% inhibition, the enzyme regains about 90% of the original activity when incubated with 10 mM metal compounds such as MnCl2, MgCl2, NiCl2 or CaCl2, the enzyme is most likely to require the metal ions for the expression of activity Corynebacterium sp.
FeCl2 1 mM, 29% remaining activity Corynebacterium sp.
HgCl2 1 mM, 23% remaining activity Corynebacterium sp.
additional information iodoacetate, dithiothreitol, 2-mercaptoethanol, sodium dodecyl sulfate or p-chloromercuribenzoate have no inhibitory effects Corynebacterium sp.
Urea enzyme preincubated in the presence of 6 M urea, dialyzed and assayed normally retains 90% activity, but if the enzyme is preincubated and assayed in the presence of 6 M urea no activity is measured Corynebacterium sp.

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ slight activation at 1 mM or 5 mM concentrations Corynebacterium sp.
Mg2+ 1 mM, 11% activation Corynebacterium sp.
Mn2+ 5 mM, 255% activity Corynebacterium sp.
additional information BaCl2 does not affect enzymatic activity Corynebacterium sp.
Ni2+ 1 mM, 13% activation Corynebacterium sp.
Zn2+ 1 mM, 175% activity Corynebacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
 gel filtration Corynebacterium sp.
28400
-
 amino acid analysis 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
-
 ?
poly-alpha-L-guluronic acid Corynebacterium sp. ALY-1
-
 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
-

Renatured (Commentary)

Renatured (Comment) Organism
6M urea collapses the circular dicroic spectral bands of the native enzyme caused by aromatic amino acids side chains and causes dissapearance of the enzyme activity, removal of the denaturant by dialysis restored the native-like spectrum and the activity, but some parts of the enzyme conformation are defective in the renaturation conditions Corynebacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-guluronosyl linkage in alginate endolyase Corynebacterium sp. ?
-
 ?
alpha-L-guluronosyl linkage in alginate endolyase Corynebacterium sp. ALY-1 ?
-
 ?
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
-
 ?
poly-alpha-L-guluronic acid
-
 Corynebacterium sp. ALY-1 unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 27000, SDS-PAGE Corynebacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Corynebacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Corynebacterium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 10 stable Corynebacterium sp.

pI Value

Organism Comment pI Value Maximum pI Value
Corynebacterium sp.
-
 7.4 7.3