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Literature summary extracted from

  • Ito, H.; Hamada, S.; Isono, N.; Yoshizaki, T.; Ueno, H.; Yoshimoto, Y.; Takeda, Y.; Matsui, H.
    Functional characteristics of C-terminal regions of starch-branching enzymes from developing seeds of kidney bean (Phaseolus vulgaris L.) (2004), Plant Sci., 166, 1149-1158.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 additional information construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2 Phaseolus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Phaseolus vulgaris Q9XIS4
-
-
2.4.1.18 Phaseolus vulgaris Q9XIS5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 chimeric enzymes Phaseolus vulgaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.18 seed
-
 Phaseolus vulgaris
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylopectin the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains Phaseolus vulgaris amylopectin with additional alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 amylose the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains Phaseolus vulgaris amylose containing alpha-1,6-glucosidic linkages
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 PvSBE1
-
 Phaseolus vulgaris
2.4.1.18 PvSBE2
-
 Phaseolus vulgaris