4.3.2.2: adenylosuccinate lyase

This is an abbreviated version!
For detailed information about adenylosuccinate lyase, go to the full flat file.

Reaction

Synonyms

adenylosuccinase, adenylosuccinate lyase, ADL, ADSL, AMPS lyase, ASASE, ASL, Glutamyl-tRNA synthetase regulatory factor, lyase, adenylosuccinate, PurB, succino AMP-lyase, succino-AMP lyase

ECTree

     4 Lyases

         4.3 Carbon-nitrogen lyases

             4.3.2 Amidine-lyases

                4.3.2.2 adenylosuccinate lyase

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Results	in table
44124	AA Sequence
8	Application
1	CAS Registry Number
22	Cloned(Commentary)
13	Crystallization (Commentary)
462	Disease/ Diagnostics
1	Expression
24	General Information
6	General Stability
74	Inhibitors
9	kcat/KM [mM/s]
3	Ki Value [mM]
72	KM Value [mM]
2	Localization
3	Metals/Ions
72	Molecular Weight [Da]
88	Natural Substrates/ Products (Substrates)
69	Organism
11	Pathway
82	PDB ID
21	pH Optimum
3	pH Range
102	Protein Variants
19	Purification (Commentary)
9	Reaction
10	Reaction Type
69	Reference
29	Source Tissue
69	Specific Activity [micromol/min/mg]
7	Storage Stability
145	Substrates and Products (Substrate)
34	Subunits
52	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
5	Temperature Stability [°C]
12	Turnover Number [1/s]

Reaction

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Reaction on EC 4.3.2.2 - adenylosuccinate lyase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

4 entries

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

5 entries

(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

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(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

kinetic and catalytic uni-bi rapid equilibrium ordered mechanism, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview

Plasmodium falciparum

O15918

691116

(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism

Bacillus subtilis

-

695003

(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism

Homo sapiens

P30566

695003

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

uni bi-ordered mechanism

Artemia sp.

-

34451

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

kinetic and catalytic mechanism, the enzyme follows a rapid equilibrium ordered bi-uni mechanism in the reverse direction in which AMP binds first to the enzyme followed by fumarate, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview

Plasmodium falciparum

O15918

691116

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism

Bacillus subtilis

-

695003

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism

Homo sapiens

P30566

695003

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP

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