6.3.2.1: pantoate-beta-alanine ligase (AMP-forming)
This is an abbreviated version!
For detailed information about pantoate-beta-alanine ligase (AMP-forming), go to the full flat file.
Word Map on EC 6.3.2.1
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6.3.2.1
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trna
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aminoacyl-trna
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aminoacylation
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coa
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glycogen
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thromboxane
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prostaglandin
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adenylate
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carboxylase
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gsh
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neurodegeneration
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nonribosomal
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acyl-coa
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carbamyl
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anticodon
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phosphorylase
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ribonucleic
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polyketide
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polyadp-ribose
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kinase-associated
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arachidonic
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purine
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ornithine
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lipogenic
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multienzyme
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lipogenesis
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indomethacin
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adp-ribose
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palmitoyl-coa
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argininosuccinate
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lipopeptide
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tx
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transcarbamylase
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acyl-coenzyme
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ifn-alpha
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thioesterase
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3-aminobenzamide
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microcystins
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cyclooxygenase
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myositis
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dermatomyositis
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interferon-induced
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dystonia
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ifn-induced
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malonyl-coa
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amber
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ifn-beta
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polymyositis
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delta-aminolevulinic
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drug development
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6-keto-pgf1
- 6.3.2.1
- trna
- aminoacyl-trna
- aminoacylation
- coa
- glycogen
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thromboxane
- prostaglandin
- adenylate
- carboxylase
- gsh
- neurodegeneration
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nonribosomal
- acyl-coa
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carbamyl
-
anticodon
- phosphorylase
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ribonucleic
- polyketide
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polyadp-ribose
-
kinase-associated
-
arachidonic
- purine
- ornithine
-
lipogenic
-
multienzyme
-
lipogenesis
- indomethacin
- adp-ribose
- palmitoyl-coa
- argininosuccinate
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lipopeptide
- tx
-
transcarbamylase
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acyl-coenzyme
- ifn-alpha
-
thioesterase
- 3-aminobenzamide
- microcystins
-
cyclooxygenase
- myositis
- dermatomyositis
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interferon-induced
- dystonia
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ifn-induced
- malonyl-coa
-
amber
-
ifn-beta
- polymyositis
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delta-aminolevulinic
- drug development
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6-keto-pgf1
Reaction
Synonyms
D-Pantoate:beta-alanine ligase (AMP-forming), MTBPS, PanC, panthotenate synthetase, Pantoate activating enzyme, pantoate-beta-alanine ligase, Pantoic-activating enzyme, pantothenate, Pantothenate synthetase, PS, PTS, Rv3602c, synthetase, Synthetase, pantothenate
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General Information
General Information on EC 6.3.2.1 - pantoate-beta-alanine ligase (AMP-forming)
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malfunction
metabolism
physiological function
additional information
alanine mutation of the catalytic sites of pantothenate synthetase causes distinct conformational changes in the ATP binding region. Analysis of the molecular mechanism of decreased affinity of the enzyme for ATP caused by alanine mutations using molecular dynamics simulations and free energy calculations
malfunction
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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alanine mutation of the catalytic sites of pantothenate synthetase causes distinct conformational changes in the ATP binding region. Analysis of the molecular mechanism of decreased affinity of the enzyme for ATP caused by alanine mutations using molecular dynamics simulations and free energy calculations
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the pantothenate synthetase is involved in the pantothenate biosynthetic pathway
metabolism
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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the pantothenate synthetase is involved in the pantothenate biosynthetic pathway
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pantothenate synthetase catalyzes the ATP-dependent formation of an amide bond between pantoate and beta-alanine
physiological function
pantothenate synthetase, an enzyme that is involved in the pantothenate biosynthetic pathway, is essential for the virulence and persistent growth of Mycobacterium tuberculosis
physiological function
the pantothenate biosynthetic pathway is essential for the persistent growth and virulence of Mycobacterium tuberculosis and one of the enzymes in the pathway
physiological function
Mycobacterium tuberculosis ATCC 27294 / ATCC 25618 / H37Rv
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the pantothenate biosynthetic pathway is essential for the persistent growth and virulence of Mycobacterium tuberculosis and one of the enzymes in the pathway
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physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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pantothenate synthetase catalyzes the ATP-dependent formation of an amide bond between pantoate and beta-alanine
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physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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pantothenate synthetase, an enzyme that is involved in the pantothenate biosynthetic pathway, is essential for the virulence and persistent growth of Mycobacterium tuberculosis
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significance and importance of conserved active site residues including His44, His47, Asn69, Gln72, Lys160 and Gln164 in substrate binding and formation of pantoyl adenylate intermediate. Molecular dynamics simulations of enzyme PS-ATP complex, substrate binding pocket and residue interactions analysis
additional information
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significance and importance of conserved active site residues including His44, His47, Asn69, Gln72, Lys160 and Gln164 in substrate binding and formation of pantoyl adenylate intermediate. Molecular dynamics simulations of enzyme PS-ATP complex, substrate binding pocket and residue interactions analysis
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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significance and importance of conserved active site residues including His44, His47, Asn69, Gln72, Lys160 and Gln164 in substrate binding and formation of pantoyl adenylate intermediate. Molecular dynamics simulations of enzyme PS-ATP complex, substrate binding pocket and residue interactions analysis
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