The role of Arg-96 in Danio rerio creatine kinase in substrate recognition and active center configuration

Uda, Kouji; Kuwasaki, Ai; Shima, Kanami; Matsumoto, Taisuke; Suzuki, Tomohiko

doi:10.1016/j.ijbiomac.2009.03.001

Cited by 16 publications

(4 citation statements)

References 24 publications

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“…The crystal structure of AK reveals that a small N-terminal domain and a large C-terminal domain are connected by a linker with the active site located in the cleft between the two domains. However, recent analysis suggests that both AK and CK consists of four dynamic domains [21]. Moreover, the importance of the interactions among the four domains has been proven in AK and CK [22].…”

Section: Introductionmentioning

confidence: 99%

Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability

Wang

et al. 2012

International Journal of Biological Macromolecules

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Section: Introductionmentioning

confidence: 99%

Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability

Wang

et al. 2012

International Journal of Biological Macromolecules

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“…Phosphagen kinases are a highly conserved family of proteins that nevertheless differ significantly with respect to their enzyme specificity and protein structure (monomeric, dimeric, and oligomeric forms of phophagen kinases are known) and distribution in the cell [59,60,61,62,63,64,65,66,67,68,69,70]. Among the most studied phosphagen kinases is the creatine kinase (EC 2.7.3.2), which is the only known phosphagen kinase to exist in vertebrates [71,72,73,74]. In contrary to creatine kinase, the arginine kinase (EC 2.7.3.3) is most widely distributed, occurring in invertebrates [75] and even in several unicellular organisms [56,76], including strains of proteobacteria like Desulfotalea psychrophila , Myxococcus xanthus , Moritella sp.…”

Section: Natural Products Containing a P–n Bond (Phosphoramidates)mentioning

confidence: 99%

Natural Products Containing ‘Rare’ Organophosphorus Functional Groups

2019

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Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P–N (phosphoramidate), P–S (phosphorothioate), and P–C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life. In this review we thoroughly categorize P–N, P–S, and P–C natural organophosphorus compounds. Information on biological source, biological activity, and biosynthesis is included, if known. This review also summarizes the role of phosphorylation on unusual amino acids in proteins (N- and S-phosphorylation) and reviews the natural phosphorothioate (P–S) and phosphoramidate (P–N) modifications of DNA and nucleotides with an emphasis on their role in the metabolism of the cell. We challenge the commonly held notion that nonphosphate organophosphorus functional groups are an oddity of biochemistry, with no central role in the metabolism of the cell. We postulate that the extent of utilization of some phosphorus groups by life, especially those containing P–N bonds, is likely severely underestimated and has been largely overlooked, mainly due to the technological limitations in their detection and analysis.

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“…Site-directed mutagenesis studies of this residue using rabbit CK and Einenia LK have shown that it has a significant effect on enzymatic activity and guanidino substrate specificity [20,21]. A recent report investigating Danio CK and Nautilus AK also showed that the 89th residue plays a key role in organizing the hydrogen-bond network between the four dynamic domains [25] of AK and CK, thereby helping provide an appropriate active center for high catalytic turnover [26].…”

Section: Amino Acid 89mentioning

confidence: 99%

Identification of the key amino acid residues in Sabellastarte arginine kinase for distinguishing chiral guanidino substrates (d- and l-arginine)

Uda

Matumoto

Suzuki

2010

Journal of Molecular Catalysis B: Enzymatic

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Arginine kinase (AK, EC 2.7.3.3) is a phosphagen kinase widely distributed in lower and higher invertebrates. Sabellastarte indica AKs (AK1 and AK2) are the only AKs that use D-arginine in addition to L-arginine as a substrate. Sabellastarte indica AKs are therefore clearly unrelated to typical AK. The purpose of this work was to identify the amino acid residues responsible for distinguishing the chirality of D-and L-arginine. The three-dimensional structure of Sabellastarte AK2 was predicted using the SWISS-MODEL automated modeling server. Two amino acids, L64 in the N-terminal flexible loop and N320 in the C-terminal flexible loop, were found to be closest to the substrate arginine. We introduced several mutations around the predicted binding site of the substrate arginine. In the L64I mutant, the affinity for L-arginine was greatly increased (9.5-fold that of the wild-type), whereas its affinity for D-arginine was increased 2.9-fold, indicating that the L64I mutant enzyme was more specific for L-arginine. On the other hand, the L64V mutant showed a 1.7-fold decrease in affinity for L-arginine, but unchanged affinity for D-arginine. Thus the L64V mutant enzyme was more specific for D-arginine. Since the replacement of amino acid residue L64 by I or V significantly affected the affinity for L-arginine or D-arginine, it can be concluded that amino acid 64 is a key residue for distinguishing D-and L-arginine. Seven mutants at position 320 (N320H, Q, D, E, R, K and A) had considerably reduced enzymatic activity (0.05 to 52% of the wild-type). The reduction in enzyme activity was more significant when D-arginine was the substrate rather than L-arginine, except for N320D, suggesting that the carbonyl oxygen of the Asn320 side chain forms a hydrogen bond with the α-amino nitrogen attached to the asymmetric carbon of the D-arginine substrate. In addition, we found that even a residue remote from the guanidino substrate binding site, such as G54 and Y89 in Sabellastarte 3 AK2, significantly affected guanidino substrate specificity.4

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The role of Arg-96 in Danio rerio creatine kinase in substrate recognition and active center configuration

Cited by 16 publications

References 24 publications

Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability

Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability

Natural Products Containing ‘Rare’ Organophosphorus Functional Groups

Identification of the key amino acid residues in Sabellastarte arginine kinase for distinguishing chiral guanidino substrates (d- and l-arginine)

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