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Literature summary extracted from

  • Duncan, K.A.; Hardin, S.C.; Huber, S.C.
    The three maize sucrose synthase isoforms differ in distribution, localization, and phosphorylation (2006), Plant Cell Physiol., 47, 959-971.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.13 production of recombinant His6-SUS2 protein (rSUS2) in Escherichia coli Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.13 cytosol SUS2 may be the housekeeping SUS isoform because it is solely cytosolic and therefore cleaves sucrose for metabolic requirements within the cytosol Zea mays 5829
-
2.4.1.13 membrane SUS-SH1 is associated with membranes Zea mays 16020
-
2.4.1.13 membrane SUS1 is associated with membranes Zea mays 16020
-
2.4.1.13 microsome SUS-SH1 is associated with microsomes Zea mays
-
-
2.4.1.13 additional information native SUS2 is not associated with membranes in vivo Zea mays
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.13 additional information Zea mays SUS2 may function to regulate SUS1 membrane association by formation of SUS1–SUS2 hetero-oligomers ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.13 Zea mays
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.13 phosphoprotein phosphorylated at a C-terminal threonine residue only in midvein Zea mays
2.4.1.13 phosphoprotein phosphorylated at a C-terminal threonine residue only in midvein. SUS-SH1 is phosphorylated in vivo at the Ser10 site in kernels Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.13 internode SUS1 is predominant in the internode cortex tissue Zea mays
-
2.4.1.13 kernel SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels Zea mays
-
2.4.1.13 kernel SUS2 is particularly abundant in kernels at various pollination stages Zea mays
-
2.4.1.13 kernel SUSSH1 is predominant in developing kernels Zea mays
-
2.4.1.13 leaf elongation zone, isoenzyme SUS-SH1 Zea mays
-
2.4.1.13 leaf elongation zone, isoenzyme SUS2. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels Zea mays
-
2.4.1.13 leaf SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination Zea mays
-
2.4.1.13 root SUS1 is predominant in etiolated shoots Zea mays
-
2.4.1.13 shoot SUS1 is predominant in etiolated shoots Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.13 additional information SUS2 may function to regulate SUS1 membrane association by formation of SUS1–SUS2 hetero-oligomers Zea mays ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.13 More SUS2 exists predominantly as a heterooligomer with SUS1 Zea mays
2.4.1.13 More SUS2 predominantly exists as a hetero-oligomer with SUS1 Zea mays
2.4.1.13 oligomer SUS-SH1 forms only homooligomers Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.4.1.13 SUS-SH1
-
 Zea mays
2.4.1.13 SUS1
-
 Zea mays
2.4.1.13 SUS2
-
 Zea mays