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2.4.2.14: amidophosphoribosyltransferase

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

Word Map on EC 2.4.2.14

Reaction

5-phospho-beta-D-ribosylamine
+
diphosphate
 +
L-glutamate
=
L-glutamine
 +
5-phospho-alpha-D-ribose 1-diphosphate
 +
H2O

Synonyms

5'-phosphoribosylpyrophosphate amidotransferase, 5-phosphoribosyl-1-pyrophosphate amidotransferase, 5-phosphoribosylpyrophosphate amidotransferase, 5-phosphororibosyl-1-pyrophosphate amidotransferase, ADE4, alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase, amido phosphoribosyltransferase, amidotransferase, phosphoribosyl pyrophosphate, APRT, ATASE, AtGPRT, Gln phosphoribosylpyrophosphate amidotransferase, glutamine 5-phosphoribosylpyrophosphate amidotransferase, glutamine phosphoribosyl pyrophosphate amidotransferase, glutamine phosphoribosylpyrophosphate amidotransferase, glutamine ribosylpyrophosphate 5-phosphate amidotransferase, GPAT, GPATase, GPRAT, GPRAT2, phosphoribose pyrophosphate amidotransferase, phosphoribosyl amidotransferase, phosphoribosyl pyrophosphate amidotransferase, phosphoribosylamidotransferase, phosphoribosyldiphosphate 5-amidotransferase, phosphoribosylpyrophosphate glutamyl amidotransferase, PPAT, PRAT, PurF

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.14 amidophosphoribosyltransferase

Engineering

Engineering on EC 2.4.2.14 - amidophosphoribosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C87A
the mutant shows strongly reduced activity compared to the wild type enzyme
D432A
the mutant shows strongly reduced activity compared to the wild type enzyme
D433A
the mutant shows strongly reduced activity compared to the wild type enzyme
R264K
increased resistance to DAS734 with >500-fold higher IC50 compared to wild-type: no inhibition by 100 microM DAS734 and no effect on reaction time course, the same allosteric inhibition by adenine nucleotides as the wild-type, Arg-264 conserved in almost every GPRAT sequence
S434A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y329A
the mutant shows strongly reduced activity compared to the wild type enzyme
A417W
-
moderate resistance to inhibition by ATP or GPT
D310V
-
almost resistant to inhibition by ATP or GTP, low concentrations of ATP plus GTP activate
K333Q
-
almost resistant to inhibition by ATP or GTP, low concentrations of ATP plus GTP activate
G331I
-
50% of wild-type glutaminase activity, reduced inhibition by GMP, enhanced inhibition by AMP
K326Q
K326Q/P410W
-
binding of GMP and AMP is abolished resulting in loss of inhibition
L415A
mutant has reduced transfer efficiency. The L415A GPATase mutant-thioester-5'-phosphoribosylpyrophosphate complex after 39 ps, shows the leakage of ammonia into bulk solution
N351A
-
approx. 50% of wild-type glutaminase activity, completely insensitive to inhibition by GMP, partially resistent to inhibition by AMP
P410W
-
reduced inhibition by AMP, strong synergistic inhibition by AMP and GMP
R26H
-
extremely labile enzyme
Y258A
-
complete loss of glutaminase and amidotransferase activity
Y258F
-
approx. 50% loss of glutaminase activity, very weak amidotransferase activity
Y329A
-
normal glutaminase activity, approx. 20% amidotransferase activity, less sensitive to GMP inhibition than wild-type
Y465A
-
100% of wild-type glutaminase activity, 28% of wild-type amidotransferase activity, inhibition by GMP and AMP is similar to wild-type
Y74A
-
complete loss of glutaminase activity, little loss of amidotransferase activity
I198V
by missense mutation A592G, purF(I198V) and variant purF(1-04) in pCA24N by two polymerase error prone PCR strategy (1. mutazyme, 2. Taq DNA polymerase in Thermopol reaction buffer) followed by second directed mutagenesis on purF(1-04) by passaging through Escherichia coli mutator strain XL1-Red leading to variant purF(2-02), mutant I198V and variants 1-04 and 2-02 improved growth of Escherichia coli JMB9 DELTA TrpF (auxotrophic for tryptophan) on medium lacking tryptophan by gained phosphoribosylanthranilate isomerase activity
N328S
recurring mutation after error-prone PCR, found in variant 1-04 of mutant I198V which also harbours mutations: I37M, A39T, E85G, P88S, N124S, I198V, K282R and one silent, Asn328 is implicated in PRPP binding and a critical residue for improving phosphoribosylanthranilate isomerase activity. Variant 2-02 has the same open reading frame as 1-04 but optimized transcription.
additional information
-
enzyme deletion mutant, auxotrophic for adenine, produces lower levels of riboflavin than wild-type