1.2.1.70: glutamyl-tRNA reductase

This is an abbreviated version!
For detailed information about glutamyl-tRNA reductase, go to the full flat file.

Word Map on EC 1.2.1.70

1.2.1.70

tetrapyrrole

chlorophyl

ala

5-aminolevulinic

heme

glutamate-1-semialdehyde

protochlorophyllide

delta-aminolevulinic

1-semialdehyde

de-etiolation

chelatase

mg-protoporphyrin

glu-trna

trna-dependent

kandleri

pchlide

gun4

glu-trnaglu

trna-bound

2,1-aminomutase

biotechnology

synthesis

Reaction

Synonyms

AtHEMA1, EC 2.7.2.13, GluRS, glutamate tRNA reductase, glutamate-specific tRNA reductase, glutamyl transfer RNA reductase, glutamyl-tRNA reductase, GluTR, GluTR1, GTR, GtrR, hemA, HEMA1, HEMA2, reductase, glutamyl-transfer ribonucleate, ZjGluTR

ECTree

1 Oxidoreductases

1.2 Acting on the aldehyde or oxo group of donors

1.2.1 With NAD⁺ or NADP⁺ as acceptor

1.2.1.70 glutamyl-tRNA reductase

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Results	in table
9	Activating Compound
28795	AA Sequence
4	Application
1	CAS Registry Number
20	Cloned(Commentary)
43	Cofactor
4	Crystallization (Commentary)
8	Expression
20	General Information
2	General Stability
3	IC50 Value
47	Inhibitors
2	KM Value [mM]
12	Localization
5	Metals/Ions
22	Molecular Weight [Da]
31	Natural Substrates/ Products (Substrates)
62	Organism
7	Pathway
9	PDB ID
3	pH Optimum
2	pI Value
39	Protein Variants
17	Purification (Commentary)
1	Reaction
52	Reference
27	Source Tissue
4	Specific Activity [micromol/min/mg]
1	Storage Stability
62	Substrates and Products (Substrate)
17	Subunits
59	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
3	Turnover Number [1/s]

Activating Compound

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Activating Compound on EC 1.2.1.70 - glutamyl-tRNA reductase

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cycloheximide

GluBP regulator

the GluTR regulator, GluTR binding protein (GluBP), spatially organizes tetrapyrrole synthesis by distributing enzyme GluTR into different suborganellar locations. GluBP belongs to a heme-binding family involved in heme metabolism. Complex structure of GluTR-GluBP from Arabidopsis thaliana, overview. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. GluBP stimulates GluTR catalytic efficiency with an approximate 3fold increase of the 5-aminolevulinic acid formation rate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde. GluBP stimulates GluTR activity and regulates GSA release

743681

glutamate-1-semialdehyde aminotransferase

2 entries

heme

Acidithiobacillus ferrooxidans

under high heme requirement for respiration levels of GluTR increase

676889

Ozone

Arabidopsis thaliana

induces expression in photosynthetic tissues

694706

protein GSAM

Acidithiobacillus ferrooxidans

B7J8J0

stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM. GluTR activity is stimulated upon formation ofa complex with protein GSAM. This effect is observed only when GluTR contained a heme/protein ratio of 1/12. GluTR activity and the stimulation of this enzyme by protein GSAM are reduced by treatment with H2O2

742701

puromycin

Arabidopsis thaliana

694706

additional information

Arabidopsis thaliana

is induced in photosynthetic tissues by oxidative stresses such as wounding

694706