Literature summary for 5.3.4.1 extracted from

Iwasaki, K.; Kamauchi, S.; Wadahama, H.; Ishimoto, M.; Kawada, T.; Urade, R.
Molecular cloning and characterization of soybean protein disulfide isomerase family proteins with nonclassic active center motifs (2009), FEBS J., 276, 4130-4141.

Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment)	Organism
GmPDIL-3a and GmPDIL-3b isozymes, cloning of mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, expression in Escherichia coli strain BL21(DE3)	Glycine max

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	both GmPDIL-3a and GmPDIL-3b are resistant to protease treatment in the absence of detergent, and are degraded when detergent is added	Glycine max

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum lumen	GmPDIL-3a and GmPDIL-3b form protein complexes in the endoplasmic reticulum	Glycine max	5788	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Glycine max

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
130000	300000	GmPDIL-3a-GmPDIL-3b protein complexes	Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Glycine max	GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Glycine max	-	cv. Jack, isozymes GmPDIL-1, GmPDIL-2, GmPDIL-3a, and GmPDIL-3b	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, from Escherichia coli strain BL21(DE3)	Glycine max

Source Tissue

Source Tissue	Comment	Organism	Textmining
cotyledon	expression of GmPDIL-3a and GmPDIL-3b in soybean cotyledons during maturation, overview	Glycine max	-
leaf	trifoliolate center leaves	Glycine max	-
additional information	GmPDIL-3a and GmPDIL-3b are ubiquitously expressed in the plant body	Glycine max	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not	Glycine max	?	-	?
additional information	recombinant GmPDIL-3a and GmPDIL-3b do not function as oxidoreductases or as molecular chaperones in vitro, although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the endoplasmic reticulum. GmPDIL-3a and GmPDIL-3b have no stimulatory effect on the oxidative refolding of RNase A by GmPDIL-1 and GmPDIL-2 when mixed together, further confirming that the functional properties of GmPDIL-3a and GmPDIL-3b are probably unique	Glycine max	?	-	?

Subunits

Subunits	Comment	Organism
More	GmPDIL-3a and GmPDIL-3b are plant endoplasmic reticulum PDI family proteins containing the nonclassic redox center motif CXXS? C	Glycine max

Synonyms

Synonyms	Comment	Organism
More	PDI and other PDI family proteins are members of the thioredoxin superfamily	Glycine max
PDI	-	Glycine max
protein disulfide isomerase	-	Glycine max

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Glycine max

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Glycine max

Expression

Organism	Comment	Expression
Glycine max	expression of GmPDIL-3a and GmPDIL-3b in the cotyledon increases during seed maturation when synthesis of storage proteins is initiated	up

General Information

General Information	Comment	Organism
physiological function	PDI and other PDI family proteins are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum	Glycine max

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Release 2023.1 (January 2023)