Primary structure of the S. cerevisiae gene encoding uridine monophosphokinase

Liljelund, Patricia; Sanni, Ambaliou; Friesen, James D.; Lacroute, François

doi:10.1016/0006-291x(89)91093-0

Cited by 25 publications

(10 citation statements)

References 26 publications

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“…As shown in Figure 1, their amino acid sequences are highly homologous to those of AKs (Liljelund et al, 1989;Wiesmuller et al, 1990;Okajima et al, 1995). In prokaryotes, there are two distinct enzymes for phosphorylation of UMP and CMP.…”

Section: Uridylate and Cytidylate Kinasesmentioning

confidence: 81%

Nucleoside Monophosphate Kinases: Structure, Mechanism, and Substrate Specificity

Yan

Tsai

1999

Advances in Enzymology - And Related Areas of Molecular Biology

131

122

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Section: Uridylate and Cytidylate Kinasesmentioning

confidence: 81%

Nucleoside Monophosphate Kinases: Structure, Mechanism, and Substrate Specificity

Yan

Tsai

1999

Advances in Enzymology - And Related Areas of Molecular Biology

131

122

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“…The amino acid sequences of adenylate kinases from various sources show considerable similarities not only to each other but also to those of UMP-CMP kinases (EC 2.7.4. t4) from yeast [3] and slime mold [4]. We have considered that the difference in substrate specificities between two different kinases is at least partly produced from the substitution of the amino acid residues located at the nucleoside monophosphate-binding site.…”

Section: Introduction Adenylate Kinase (Ec 2743) Catalyzes the Revmentioning

confidence: 99%

Site‐directed mutagenesis of AMP‐binding residues in adenylate kinase Alteration of substrate specificity

1993

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Adenylate kinase is highly specific for AMP as phosphoryl acceptor. We have found that the replacement of Thr 39 by Ala in the chicken muscle enzyme, alone or together with the replacement of Leu 66 by Ile, caused remarkable increases in CMP and UMP activities with a concomitant decrease in AMP activity; therefore, the resulting mutant enzymes show CMP and UMP activities/AMP activity ratios much higher than the wild-type enzyme. The mutant enzyme in which Ala is substituted for Thr 39 has a Vma x value for CMP comparable to that of CMP-UMP kinase.

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“…Much less is known on the other members of NMP kinase family. Apparently they belong to the adenylate kinase paradigm (Liljelund et al, 1989;Wiesmü ller et al, 1990;Konrad, 1992;Mü ller-Dieckmann and Schulz, 1994) exhibiting sequence similarities and related three-dimensional structure. However, UMP kinase from Escherichia coli and probably from other enteric bacteria deviate from this paradigm.…”

mentioning

confidence: 99%

CMP Kinase from Escherichia coli Is Structurally Related to Other Nucleoside Monophosphate Kinases

Bucurenci

Sakamoto

Briozzo

et al. 1996

Journal of Biological Chemistry

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CMP kinase from Escherichia coli is a monomeric protein of 225 amino acid residues. The protein exhibits little overall sequence similarities with other known NMP kinases. However, residues involved in binding of substrates and/or in catalysis were found conserved, and sequence comparison suggested conservation of the global fold found in adenylate kinases or in several CMP/UMP kinases. The enzyme was purified to homogeneity, crystallized, and analyzed for its structural and catalytic properties. The crystals belong to the hexagonal space group P6 3 , have unit cell parameters a ‫؍‬ b ‫؍‬ 82.3 Å and c ‫؍‬ 60.7 Å, and diffract x-rays to a 1.9 Å resolution. The bacterial enzyme exhibits a fluorescence emission spectrum with maximum at 328 nm upon excitation at 295 nm, which suggests that the single tryptophan residue (Trp 30 ) is located in a hydrophobic environment. Substrate specificity studies showed that CMP kinase from E. coli is active with ATP, dATP, or GTP as donors and with CMP, dCMP, and arabinofuranosyl-CMP as acceptors. This is in contrast with CMP/UMP kinase from Dictyostelium discoideum, an enzyme active on CMP or UMP but much less active on the corresponding deoxynucleotides. Binding of CMP enhanced the affinity of E. coli CMP kinase for ATP or ADP, a particularity never described in this family of proteins that might explain inhibition of enzyme activity by excess of nucleoside monophosphate.

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Primary structure of the S. cerevisiae gene encoding uridine monophosphokinase

Cited by 25 publications

References 26 publications

Nucleoside Monophosphate Kinases: Structure, Mechanism, and Substrate Specificity

Nucleoside Monophosphate Kinases: Structure, Mechanism, and Substrate Specificity

Site‐directed mutagenesis of AMP‐binding residues in adenylate kinase Alteration of substrate specificity

CMP Kinase from Escherichia coli Is Structurally Related to Other Nucleoside Monophosphate Kinases

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