Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.59 extracted from

  • Zhang, Y.; Launay, H.; Liu, F.; Lebrun, R.; Gontero, B.
    Interaction between adenylate kinase 3 and glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii (2018), FEBS J., 285, 2495-2503 .
    View publication on PubMed
Search for more literature for 1.2.1.59

General Stability

General Stability Organism
ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. This ability is linked to the presence of the CP12-like extension of ADK3 as no protection is observed when this part is removed Chlamydomonas reinhardtii

Inhibitors

Inhibitors Comment Organism Structure
protein CP12 the enzyme GapDH interacts with the intrinsically disordered protein CP12, when oxidized but not when reduced, in chloroplasts forming a stable complex. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. CP12 acts as a chaperone for GAPDH. The NADH-dependent activity of the chloroplast GAPDH is not affected by incubation at 4°C, for between 1 and 14 h, with either oxidized ADK3 (OxADK3) or ADK3-DELTACP12 at a ratio of 2 :1 (dimeric ADK : tetrameric GAPDH). When incubated with ADK3, about 63% of the NADPH-dependent activity of GAPDH disappear and this activity is recovered by DTT. Enzyme-ADK3 interaction analysis, overview Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Chlamydomonas reinhardtii 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Chlamydomonas reinhardtii
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NADP+ Chlamydomonas reinhardtii
-
 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii P50362 NADP-dependent glyceraldehydephosphate dehydrogenase subunit A
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Chlamydomonas reinhardtii 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Chlamydomonas reinhardtii 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 ?
additional information glyceraldehyde-3-phosphate dehydrogenase from chloroplasts has a dual cofactor specificity and can use both NADPH and NADH Chlamydomonas reinhardtii ?
-
-

Subunits

Subunits Comment Organism
homotetramer in Chlamydomonas reinhardtii, the chloroplast GAPDH is a homotetrameric A4-isoform that lacks regulatory cysteine residues found in the B subunit of the heterotetrameric A2B2-GAPDH isoform Chlamydomonas reinhardtii

Synonyms

Synonyms Comment Organism
chloroplast glyceraldehyde-3-phosphate dehydrogenase
-
 Chlamydomonas reinhardtii
GapA
-
 Chlamydomonas reinhardtii
GAPDH
-
 Chlamydomonas reinhardtii
NADP-dependent glyceraldehydephosphate dehydrogenase
-
 Chlamydomonas reinhardtii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Chlamydomonas reinhardtii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
 the NADH-dependent activity of the chloroplast GAPDH is not affected by incubation at 4°C, for between 1 and 14 h, with either oxidized ADK3 (OxADK3) or ADK3-DELTACP12 at a ratio of 2:1 (dimeric ADK:tetrameric GAPDH) Chlamydomonas reinhardtii
43
-
 upon heat-treatment, GAPDH becomes denatured and precipitated but ADK3 greatly improves its thermal stability, decreasing its aggregation and protecting its activity at 43°C. This ability is linked to the presence of the CP12-like extension of ADK3 as no protection is observed when this part is removed Chlamydomonas reinhardtii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7 7.9 assay at Chlamydomonas reinhardtii

Cofactor

Cofactor Comment Organism Structure
additional information glyceraldehyde-3-phosphate dehydrogenase from chloroplasts has a dual cofactor specificity and can use both NADPH and NADH Chlamydomonas reinhardtii
NAD+
-
 Chlamydomonas reinhardtii
NADP+
-
 Chlamydomonas reinhardtii

General Information

General Information Comment Organism
malfunction the enzyme GapDH interacts with the intrinsically disordered protein CP12, when oxidized but not when reduced, in chloroplasts forming a stable complex. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. The ADK3-GAPDH bienzyme complex is unable to recruit phosphoribulokinase (PRK), in contrast with the ternary complex formed between GAPDH-CP12 and PRK. The interaction between ADK3 and GAPDH might be a mechanism to regulate the crucial ATP: NADPH ratio within chloroplasts to optimize the Calvin-Benson cycle during rapid fluctuation in environmental resources Chlamydomonas reinhardtii
additional information ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH Chlamydomonas reinhardtii
physiological function in Chlamydomonas reinhardtii, the chloroplast GAPDH is a homotetrameric A4-isoform that lacks regulatory cysteine residues found in the B subunit of the heterotetrameric A2B2-GAPDH isoform. Whereas A2B2-GAPDHs from higher plants are autonomously regulated, CP12 is required to confer redox regulation to the algal A4-GAPDH. In contrast, the CP12-like tail bearing two cysteine residues present on ADK3 is not involved in its redoxregulation Chlamydomonas reinhardtii