BRENDA - Enzyme Database show
show all sequences of 2.5.1.44

The formation of homospermidine by an enzyme from Rhodopseudomonas viridis

Tait, G.H.; Biochem. Soc. Trans. 7, 199-200 (1979)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
1,3-Diaminopropane
strong competitive inhibitor, Ki: 0.002 mM
Blastochloris viridis
1,5-Diaminopentane
weak inhibition
Blastochloris viridis
additional information
4-aminobutyraldehyde, postulated intermediate, no inhibition
Blastochloris viridis
NADH
competitive inhibitor, Ki: 0.0015 mM
Blastochloris viridis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0025
-
NAD+
-
Blastochloris viridis
0.2
-
putrescine
-
Blastochloris viridis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
optimal activity with 40 mM, Na+ and Rb+ are less effective
Blastochloris viridis
Na+
less effective than K+ in activation
Blastochloris viridis
Rb+
less effective than K+ in activation
Blastochloris viridis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
73000
-
gel filtration
Blastochloris viridis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 putrescine
Blastochloris viridis
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
sym-homospermidine + NH3
-
Blastochloris viridis
?
2 putrescine
Blastochloris viridis N.C.I.B. 10028
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
sym-homospermidine + NH3
-
Blastochloris viridis N.C.I.B. 10028
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Blastochloris viridis
-
accession no. L77975; N.C.I.B. 10028
-
Blastochloris viridis N.C.I.B. 10028
-
N.C.I.B. 10028
-
Purification (Commentary)
Commentary
Organism
200fold
Blastochloris viridis
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture medium
crude extract after ultrasonication and centrifugation
Blastochloris viridis
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 putrescine
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
288697
Blastochloris viridis
sym-homospermidine + NH3
-
288697
Blastochloris viridis
?
2 putrescine
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
288697
Blastochloris viridis N.C.I.B. 10028
sym-homospermidine + NH3
-
288697
Blastochloris viridis N.C.I.B. 10028
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
cannot be replaced by NADP+, NADPH, NADH; required in catalytic amounts with a Km-value of 0.0025 mM
Blastochloris viridis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
cannot be replaced by NADP+, NADPH, NADH; required in catalytic amounts with a Km-value of 0.0025 mM
Blastochloris viridis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,3-Diaminopropane
strong competitive inhibitor, Ki: 0.002 mM
Blastochloris viridis
1,5-Diaminopentane
weak inhibition
Blastochloris viridis
additional information
4-aminobutyraldehyde, postulated intermediate, no inhibition
Blastochloris viridis
NADH
competitive inhibitor, Ki: 0.0015 mM
Blastochloris viridis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0025
-
NAD+
-
Blastochloris viridis
0.2
-
putrescine
-
Blastochloris viridis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
optimal activity with 40 mM, Na+ and Rb+ are less effective
Blastochloris viridis
Na+
less effective than K+ in activation
Blastochloris viridis
Rb+
less effective than K+ in activation
Blastochloris viridis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
73000
-
gel filtration
Blastochloris viridis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 putrescine
Blastochloris viridis
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
sym-homospermidine + NH3
-
Blastochloris viridis
?
2 putrescine
Blastochloris viridis N.C.I.B. 10028
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
sym-homospermidine + NH3
-
Blastochloris viridis N.C.I.B. 10028
?
Purification (Commentary) (protein specific)
Commentary
Organism
200fold
Blastochloris viridis
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture medium
crude extract after ultrasonication and centrifugation
Blastochloris viridis
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 putrescine
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
288697
Blastochloris viridis
sym-homospermidine + NH3
-
288697
Blastochloris viridis
?
2 putrescine
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
288697
Blastochloris viridis N.C.I.B. 10028
sym-homospermidine + NH3
-
288697
Blastochloris viridis N.C.I.B. 10028
?
Other publictions for EC 2.5.1.44
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739378
Lopez-Gomez
-
Homospermidine synthase contri ...
Rhizobium tropici, Rhizobium tropici Rt CIAT899
Plant Soil
404
413-425
2016
-
-
1
-
1
-
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
739672
Krossa
Comprehensive structural chara ...
Blastochloris viridis
Sci. Rep.
6
19501
2016
-
-
-
1
2
-
-
-
-
1
-
2
-
5
-
-
-
2
-
-
-
-
6
1
-
-
-
-
1
-
-
2
-
-
-
-
-
-
2
1
2
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
6
1
-
-
-
-
1
-
-
-
-
3
3
-
-
-
739108
Li
Different polyamine pathways f ...
Paramecium tetraurelia, Paramecium tetraurelia d4-2
Mol. Microbiol.
97
791-807
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
704662
Shaw
Evolution and multifarious hor ...
Acinetobacter tartarogenes, Blastochloris viridis, Bradyrhizobium japonicum, Opitutus terrae, Paramecium tetraurelia, Ralstonia phage phiRSL1, Rhizobium leguminosarum
J. Biol. Chem.
285
14711-14723
2010
-
-
7
-
-
-
-
3
-
-
-
-
-
15
-
-
-
-
-
-
-
-
7
-
6
-
-
3
6
-
-
7
-
-
-
-
-
7
7
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
7
-
6
-
-
3
6
-
-
-
-
1
1
-
3
3
288701
Tholl
Purification, molecular clonin ...
Blastochloris viridis
Eur. J. Biochem.
240
373-379
1996
-
-
1
-
-
-
-
1
-
-
3
1
-
6
-
-
1
-
-
1
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
3
1
-
-
-
1
-
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
288702
Ober
-
Homospermidine synthase of Rho ...
Blastochloris viridis
J. Gen. Appl. Microbiol.
42
411-420
1996
-
-
-
-
-
-
-
4
-
1
-
1
-
1
-
-
-
-
-
1
-
-
9
-
1
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
4
-
1
-
1
-
-
-
-
-
1
-
-
9
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
288699
Böttcher
-
Biosynthesis of pyrrolizidine ...
Blastochloris viridis
Can. J. Chem.
72
80-85
1994
-
-
-
-
-
-
-
3
-
-
-
1
-
1
-
-
1
-
-
1
1
1
9
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
1
-
-
-
1
-
1
1
1
9
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
288700
Yamamoto
Purification and characterizat ...
Acinetobacter tartarogenes
J. Biochem.
114
45-49
1993
-
-
-
-
-
-
3
1
-
1
2
1
-
6
-
-
1
-
-
-
1
1
1
1
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
1
-
1
2
1
-
-
-
1
-
-
1
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
288698
Srivenugopal
Enzymic synthesis of sym-homos ...
Lathyrus sativus, Santalum album
Biochem. J.
190
461-464
1980
-
-
-
-
-
-
4
1
-
-
1
2
-
2
-
-
1
-
-
2
2
-
2
-
1
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
1
-
-
1
2
-
-
-
1
-
2
2
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
288697
Tait
The formation of homospermidin ...
Blastochloris viridis, Blastochloris viridis N.C.I.B. 10028
Biochem. Soc. Trans.
7
199-200
1979
-
-
-
-
-
-
4
2
-
3
1
2
-
2
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
2
-
3
1
2
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
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-
-
-
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