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Literature summary for 3.4.22.34 extracted from

  • Scott, M.P.; Jung, R.; Muntz, K.; Nielsen, N.C.
    A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean (1992), Proc. Natl. Acad. Sci. USA, 89, 658-662.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.34

Activating Compound

Activating Compound Comment Organism Structure
DTT stimulates Glycine max

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Glycine max
Hg2+
-
 Glycine max
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
-
 Glycine max
additional information alpha2-macroglobulin; leupeptin; not: EDTA; pepstatin Glycine max

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 soybean, HPLC size exclusion chromatography Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Glycine max

Purification (Commentary)

Purification (Comment) Organism
-
 Glycine max

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Glycine max

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Proglycinin + H2O cleavage takes place between the conserved Asn and Gly residues Glycine max ?
-
 ?
Prolegumin + H2O cleavage takes place between the conserved Asn and Gly residues Glycine max ?
-
 ?