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Literature summary for 4.2.2.11 extracted from

  • Sim, P.; Furusawa, G.; Teh, A.
    Functional and structural studies of a multidomain alginate lyase from Persicobacter sp. CCB-QB2 (2017), Sci. Rep., 7, 13656 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.2.11

Inhibitors

Inhibitors Comment Organism Structure
EDTA 1 mM, 37% of initial activity Persicobacter sp. CCB-QB2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.39
-
 alginate truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C Persicobacter sp. CCB-QB2
1.46
-
 alginate truncated protein lacking the CBM16 domain, pH 7.0, 23°C Persicobacter sp. CCB-QB2
2.42
-
 alginate wild-type, pH 7.0, 23°C Persicobacter sp. CCB-QB2

Organism

Organism UniProt Comment Textmining
Persicobacter sp. CCB-QB2 A0A3B6UEP6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alginate best substrate Persicobacter sp. CCB-QB2 unsaturated algino-oligosaccharides
-
 ?
poly(alpha-(1,4)-L-guluronate) about 60% of the activity with alginate Persicobacter sp. CCB-QB2 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
 ?
poly(beta-(1,4)-D-mannuronate) reaction of EC 4.2.2.3, about 30% of the activity with alginate Persicobacter sp. CCB-QB2 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
 ?

Synonyms

Synonyms Comment Organism
AlyQ
-
 Persicobacter sp. CCB-QB2
WP_053404615 locus name Persicobacter sp. CCB-QB2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Persicobacter sp. CCB-QB2

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30
-
 30% of maximum activity Persicobacter sp. CCB-QB2

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.24
-
 alginate truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C Persicobacter sp. CCB-QB2
10.4
-
 alginate truncated protein lacking the CBM16 domain, pH 7.0, 23°C Persicobacter sp. CCB-QB2
32.2
-
 alginate wild-type, pH 7.0, 23°C Persicobacter sp. CCB-QB2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Persicobacter sp. CCB-QB2

pH Range

pH Minimum pH Maximum Comment Organism
4 6 about 60% of maximum acivity Persicobacter sp. CCB-QB2

General Information

General Information Comment Organism
physiological function alginate lyase consists of three domains, i.e. a carbohydrate-binding domain, a family 32 CBM domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). The CBM32 domain does not contribute to enhancing AlyQ's activity under the assayed conditions but can bind to cleaved but not intact alginate. The CBM32 and catalytic domains do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1 Persicobacter sp. CCB-QB2

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.64
-
 alginate truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C Persicobacter sp. CCB-QB2
7.12
-
 alginate truncated protein lacking the CBM16 domain, pH 7.0, 23°C Persicobacter sp. CCB-QB2
13.3
-
 alginate wild-type, pH 7.0, 23°C Persicobacter sp. CCB-QB2