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Literature summary for 3.2.1.68 extracted from

  • Lin, Q.; Facon, M.; Putaux, J.L.; Dinges, J.R.; Wattebled, F.; DHulst, C.; Hennen-Bierwagen, T.A.; Myers, A.M.
    Function of isoamylase-type starch debranching enzymes ISA1 and ISA2 in the Zea mays leaf (2013), New Phytol., 200, 1009-1021.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons Zea mays

Protein Variants

Protein Variants Comment Organism
additional information generation of mutant isa2-339 Zea mays
additional information generation of mutant su1-4582 Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Zea mays 9507
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
x * 75000, SDS-PAGE Zea mays
80000
-
x * 80000, about, SDS-PAGE Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
gene isa2
-
Zea mays B6U0X5 gene su-1
-

Purification (Commentary)

Purification (Comment) Organism
native subunit ISA2 from leaves by anion exchange chromatography, ultrafiltration, and gel filtration, separation from subunit ISA1 Zea mays
native subunit ISAI from leaves by anion exchange chromatography, ultrafiltration, and gel filtration, separation from subunit ISA2 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm the ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects Zea mays
-
leaf three ISA activity forms are observed in leaves, two ISA1/ISA2 heteromultimers and one ISA1 homomultimer. ISA1 homomultimer activity exists in mutants lacking ISA2. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2. The data imply that both the ISA1 homomultimer and ISA1/ISA2 heteromultimer function in the maize leaf. The ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O
-
Zea mays ?
-
?
maize starch + H2O
-
Zea mays ?
-
?

Subunits

Subunits Comment Organism
? x * 75000, SDS-PAGE Zea mays
? x * 80000, about, SDS-PAGE Zea mays

Synonyms

Synonyms Comment Organism
ISA1
-
Zea mays
ISA2
-
Zea mays
isoamylase-type starch debranching enzyme 1
-
Zea mays
isoamylase-type starch debranching enzyme 2
-
Zea mays

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycosyl hydrolase family 13 GH13, and harbors a carbohydrate-binding module family 48 (CBM48) domain Zea mays
malfunction the ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2, mutant phenotypes, overview Zea mays
malfunction the ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2. Plastids from maize leaves lacking ISA2 exhibit a nearly normal appearance with the exception that starch granules appear to be slightly smaller than in wild-type, mutant phenotypes, overview Zea mays