Information on EC 2.3.1.128 - ribosomal-protein-alanine N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.128
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RECOMMENDED NAME
GeneOntology No.
ribosomal-protein-alanine N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
A group of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88, peptide alpha-N-acetyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase
A group of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88, peptide alpha-N-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
113383-52-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12
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Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + Ala-Arg-Tyr-Phe-Arg-Arg
CoA + ?
show the reaction diagram
a peptide substrate (S181-6) representing the first six N-terminal residues of S18 (minus the initiator methionine) is used as a substrate
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?
acetyl-CoA + ribosomal-protein L-alanine
CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + ribosomal-protein L-alanine
CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.316
Ala-Arg-Tyr-Phe-Arg-Arg
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Q8ZJW4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio fischeri (strain ATCC 700601 / ES114)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18230
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calculated from amino acid sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of RimI is determined in complex with CoA, AcCoA, and a CoA-S-acetyl-ARYFRR bisubstrate inhibitor. The structures are consistent with a direct nucleophilic addition-elimination mechanism with Glu103 and Tyr115 acting as the catalytic base and acid, respectively. The RimI-bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography and gel filtration using a HiPrep 26/60 Sephacryl S-200 high-resolution gel filtration column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a C-terminal decahistidine tagged fusion protein in Escherichia coli
gene rimI encoding enzyme acetylating ribosomal protein S18 cloned into a mini-F plasmid pRE432 and sequenced
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Show AA Sequence (7458 entries)
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