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Literature summary extracted from

  • Banerjee, S.; Agrawal, M.J.; Mishra, D.; Sharan, S.; Balaram, H.; Savithri, H.S.; Murthy, M.R.
    Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme (2014), FEBS J., 281, 1642-1658.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.2 phylogenetic analysis Mycobacterium tuberculosis
4.3.2.2 phylogenetic analysis Mycolicibacterium smegmatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.2 purified enzyme, X-ray diffraction structure determination and analysis at 2.16 A resolution Mycolicibacterium smegmatis
4.3.2.2 purified enzyme, X-ray diffraction structure determination is not possible Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.2.2 additional information
-
 additional information Michaelis-Menten kinetics Mycobacterium tuberculosis
4.3.2.2 additional information
-
 additional information Michaelis-Menten kinetics Mycolicibacterium smegmatis
4.3.2.2 0.0437
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycolicibacterium smegmatis
4.3.2.2 0.2042
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide Mycobacterium tuberculosis
-
 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide Mycolicibacterium smegmatis
-
 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 additional information Mycobacterium tuberculosis the activity of the Mycobacterium tuberculosis enzyme is particularly low ?
-
 ?
4.3.2.2 succinyladenosine monophosphate Mycobacterium tuberculosis
-
 AMP + fumarate
-
 r
4.3.2.2 succinyladenosine monophosphate Mycolicibacterium smegmatis
-
 AMP + fumarate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Mycobacterium tuberculosis
-
-
-
4.3.2.2 Mycolicibacterium smegmatis A0R4I6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide
-
 Mycobacterium tuberculosis 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide
-
 Mycolicibacterium smegmatis 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 additional information the activity of the Mycobacterium tuberculosis enzyme is particularly low Mycobacterium tuberculosis ?
-
 ?
4.3.2.2 succinyladenosine monophosphate
-
 Mycobacterium tuberculosis AMP + fumarate
-
 r
4.3.2.2 succinyladenosine monophosphate
-
 Mycolicibacterium smegmatis AMP + fumarate
-
 r

Subunits

EC Number Subunits Comment Organism
4.3.2.2 homotetramer the enzyme forms a tight tetramer with three independent stable interfaces, protomer flexibility and partial disorder. The C3 loop is mostly disordered in subunits B and C, the Mycobacterium smegmatis enzyme is the first reported unliganded enzyme structure in which the C3 loop is ordered at least partially Mycolicibacterium smegmatis

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 ASL
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.2.2 37
-
 assay at Mycobacterium tuberculosis
4.3.2.2 37
-
 assay at Mycolicibacterium smegmatis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.2.2 0.1
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycobacterium tuberculosis
4.3.2.2 0.7
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.2.2 7.6
-
-
 Mycobacterium tuberculosis
4.3.2.2 8
-
-
 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
4.3.2.2 evolution the enzyme structurally resembles the enzymes of the aspartase/fumarase superfamily, conserved flexible C3 loop, phylogenetic analysis Mycobacterium tuberculosis
4.3.2.2 evolution the enzyme structure adheres to the fold of the enzymes of the aspartase/fumarase superfamily, conserved flexible C3 loop, phylogenetic analysis Mycolicibacterium smegmatis
4.3.2.2 additional information homology modeling of the enzyme structure using the Mycobacterium smegmatis enzyme structure as a template, comparison to the human enzyme structure and other enzymes, structure-function relationship analysis based on the Mycobacterium smegmatis enzyme structure, active site residues, overview Mycobacterium tuberculosis
4.3.2.2 additional information structure-function relationship analysis, active site residues, overview Mycolicibacterium smegmatis
4.3.2.2 physiological function a housekeeping enzyme Mycobacterium tuberculosis
4.3.2.2 physiological function a housekeeping enzyme Mycolicibacterium smegmatis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.2.2 0.5
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycobacterium tuberculosis
4.3.2.2 16.02
-
 succinyladenosine monophosphate pH 7.6, 37°C Mycolicibacterium smegmatis