Literature summary for 2.4.1.18 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.

Search for more literature for 2.4.1.18

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Phaseolus vulgaris	Q9XIS4	-	-
Phaseolus vulgaris	Q9XIS5	-	-

Purification (Commentary)

Purification (Comment)	Organism
chimeric enzymes	Phaseolus vulgaris

Source Tissue

Source Tissue	Comment	Organism	Textmining
seed	-	Phaseolus vulgaris	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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

Synonyms	Comment	Organism
PvSBE1	-	Phaseolus vulgaris
PvSBE2	-	Phaseolus vulgaris

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)