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Information on EC 2.5.1.152 - D-histidine 2-aminobutanoyltransferase and Organism(s) Staphylococcus aureus and UniProt Accession A0A0H3JXA8

for references in articles please use BRENDA:EC2.5.1.152
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IUBMB Comments
The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
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Staphylococcus aureus
UNIPROT: A0A0H3JXA8
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
sanas, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-histidine 2-aminobutanoyltransferase
UniProt
nicotianamine synthase-like enzyme
UniProt
cntL
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:D-histidine N-[(3S)-3-amino-3-carboxypropyl]-transferase
The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + D-histidine
N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
show the reaction diagram
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?
additional information
?
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SaNAS is specific for D-histidine. Coupled assay with enzyme staphylopine synthase from Staphylococcus aureus (SaODH, EC 1.5.1.52). Substrate specificities, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + D-histidine
N-[(3S)-3-amino-3-carboxypropyl]-D-histidine + S-methyl-5'-thioadenosine
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
D-histidine
pH 8.0, 22°C, recombinant His-tagged enzyme
additional information
additional information
Michaelis-Menten steady-state kinetics, stopped flow spectrometry
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.298
D-histidine
pH 8.0, 22°C, recombinant His-tagged enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.92
D-histidine
pH 8.0, 22°C, recombinant His-tagged enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2
purified recombinant His-tagged enzyme, with pyruvate and D-histidine, NADPH oxidation, pH 8,0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the NADPH is oxidized to NADP+ by the Staphylococcus aureus SaODH (EC 1.5.1.52) in the presence of nicotianamine synthase (PaNAS), S-adenosyl-L-methionine (SAM,) and the correct amino acid and 2-oxo acid substrates. The combination of D-histidine and pyruvate results in significant oxidation of NADPH by SaODH
physiological function
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme SaNAS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cntL, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghssein, G.; Brutesco, C.; Ouerdane, L.; Fojcik, C.; Izaute, A.; Wang, S.; Hajjar, C.; Lobinski, R.; Lemaire, D.; Richaud, P.; Voulhoux, R.; Espaillat, A.; Cava, F.; Pignol, D.; Borezee-Durant, E.; Arnoux, P.
Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus
Science
352
1105-1109
2016
Staphylococcus aureus (A0A0H3JXA8), Staphylococcus aureus ATCC 700699 (A0A0H3JXA8)
Manually annotated by BRENDA team
McFarlane, J.S.; Lamb, A.L.
Biosynthesis of an opine metallophore by Pseudomonas aeruginosa
Biochemistry
56
5967-5971
2017
Staphylococcus aureus (A0A0H3JXA8), Staphylococcus aureus ATCC 700699 (A0A0H3JXA8), Staphylococcus aureus Mu50 (A0A0H3JXA8)
Manually annotated by BRENDA team