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Literature summary for 3.2.1.1 extracted from

  • Cipolla, A.; Delbrassine, F.; Da Lage, J.L.; Feller, G.
    Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases (2012), Biochimie, 94, 1943-1950.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.065
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Sus scrofa
0.13
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Drosophila melanogaster
0.223
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Pseudoalteromonas haloplanktis
0.26
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Thermobifida fusca

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster P08144 isoform Amy-p
-
Pseudoalteromonas haloplanktis P29957
-
-
Sus scrofa P00690 isoform Amy2
-
Thermobifida fusca Q47R94
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
-
Sus scrofa 4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
-
Thermobifida fusca 4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
-
Pseudoalteromonas haloplanktis 4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
?
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene + H2O
-
Drosophila melanogaster 4-nitrophenol + 4,6-O-ethylidene-[G7]-alpha-D-maltoheptaose
-
?
starch + H2O
-
Sus scrofa ?
-
?
starch + H2O
-
Thermobifida fusca ?
-
?
starch + H2O
-
Pseudoalteromonas haloplanktis ?
-
?
starch + H2O
-
Drosophila melanogaster ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
29
-
-
Pseudoalteromonas haloplanktis
54
-
-
Sus scrofa
54
-
-
Drosophila melanogaster
72
-
-
Thermobifida fusca

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
44.1
-
melting temperature Pseudoalteromonas haloplanktis
57.7
-
melting temperature Drosophila melanogaster
65
-
melting temperature Sus scrofa
74
-
melting temperature Thermobifida fusca

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
153
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Thermobifida fusca
179
-
starch pH not specified in the publication, 5°C Pseudoalteromonas haloplanktis
280
-
starch pH not specified in the publication, 20°C Drosophila melanogaster
291
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Sus scrofa
364
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Drosophila melanogaster
518
-
starch pH not specified in the publication, 37°C Sus scrofa
675
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Pseudoalteromonas haloplanktis
1457
-
starch pH not specified in the publication, 55°C Thermobifida fusca

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.5
-
Sus scrofa
7.2 7.5
-
Thermobifida fusca
7.2 7.5
-
Pseudoalteromonas haloplanktis
7.2 7.5
-
Drosophila melanogaster

General Information

General Information Comment Organism
physiological function comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism Sus scrofa
physiological function comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism Thermobifida fusca
physiological function comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism Pseudoalteromonas haloplanktis
physiological function comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism Drosophila melanogaster

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
600
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Thermobifida fusca
2800
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Drosophila melanogaster
3000
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Pseudoalteromonas haloplanktis
4500
-
4-nitrophenyl alpha-D-maltoheptaoside-4,6-O-ethylidene pH not specified in the publication, 25°C Sus scrofa