Literature summary for 2.3.1.20 extracted from

Xu, Y.; Caldo, K.M.P.; Falarz, L.; Jayawardhane, K.; Chen, G.
Kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein (2020), Plant J., 102, 856-871.

Search for more literature for 2.3.1.20

Cloned(Commentary)

Cloned (Comment)	Organism
gene DGAT1, transient expression of N-terminally truncated CzDGAT1 variants and of the ACBP-fused versions in Nicotiana benthamiana leaves for lipid production using the transformation method via Agrobacterium tumefaciens GV3101 cells	Chromochloris zofingiensis

Protein Variants

Protein Variants	Comment	Organism
additional information	kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein AtACBP6 from Arabidosis thaliana (UniProt ID P57752), generation of N-terminally truncated DGAT1 versions as fusion proteins: ACBP-CzDGAT11-550, ACBP-CzDGAT181-550, and ACBP-CzDGAT1107-550. The coding sequences of AtACBP6 and variant CzDGAT1s are individually amplified and the resulting amplicons are fused using overlap extension PCR. Fusion of ACBP to the N-terminus of the full-length CzDGAT1 not only augments the protein accumulation levels in yeast and tobacco leaves but also kinetically improves the enzyme. ACBP-fused DGAT1 is more effective in improving the oil contents of yeast cells and vegetative tissues than the native DGAT1	Chromochloris zofingiensis

Inhibitors

Inhibitors	Comment	Organism	Structure
acyl-CoA	substrate inhibition of DGAT1, acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana slightly enhances the substrate inhibition of DGAT1 at the acyl-CoA concentrations above 0.01 mM	Chromochloris zofingiensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acyl-CoA + 1,2-diacyl-sn-glycerol	Chromochloris zofingiensis	-	CoA + 1,2,3-triacylglycerol	-	?

Organism

Organism	UniProt	Comment	Textmining
Chromochloris zofingiensis	A0A411PNL0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acyl-CoA + 1,2-diacyl-sn-glycerol	-	Chromochloris zofingiensis	CoA + 1,2,3-triacylglycerol	-	?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol	-	Chromochloris zofingiensis	CoA + 1,2,3-trioleoylglycerol	-	?

Synonyms

Synonyms	Comment	Organism
CzDGAT1B	-	Chromochloris zofingiensis
DGAT1	-	Chromochloris zofingiensis
diacylglycerol acyltransferase 1	-	Chromochloris zofingiensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Chromochloris zofingiensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Chromochloris zofingiensis

General Information

General Information	Comment	Organism
evolution	the evolutionary and sequence analyses revealed that CzDGAT1 and other green microalgal DGAT1 are closely related to the plant DGAT1 clade. But algal DGAT1 may have different evolutionary and structural features from plant and animal DGAT1 with respect to the hydrophilic N-terminal domain. This domain is predicted to be present in a less disordered state in CzDGAT1 than that of animal/plant DGAT1. The two isoforms of DGAT1 from the green microalga Chromochloris zofingiensis have very distinct features. They share 39.9% amino acid pairwise identity and have very different lengths mainly attributable to the variable N-terminal regions	Chromochloris zofingiensis
malfunction	although the N-terminal domain of algal DGAT1 is not necessary for acyltransferase activity of CzDGAT1, its removal leads to huge decreases in CzDGAT1 enzyme activity, which cannot be restored by fusion with an acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana. Replacement of the N-terminal region by ACBP in CzDGAT1 (ACBP-fused CzDGAT1107-550) is not able to restore or improve the enzyme activity suggesting that the N-terminus may function as a regulatory domain rather than as an acyl-CoA binding site	Chromochloris zofingiensis

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)