ライフサイエンスコーパス: SHMT

1 SHMT also catalyzes the folate-independent retroaldol cl

2 SHMT catalyses interconversion of serine and glycine whi

3 SHMT enzymes are the major source of the one-carbon unit

4 SHMT is crucial for deoxythymidylate biosynthesis and a

5 SHMT is involved in the penultimate step of thymidylate

6 SHMT is present in eukaryotic cells as mitochondrial SHM

7 SHMT requires both pyridoxal phosphate (PLP) and tetrahy

8 SHMT tetramers have surface charge distributions which s

9 ers for (6S)-5,10-CH(2)-H(4)PteGlu(5) for an SHMT from any organism.

10 t) values for 5,10-CH(2)-H(4)PteGlu(5) of an SHMT from Arabidopsis thaliana.

11 ves incubating [2-3H]glycine, H4PteGlun, and SHMT for 3 min followed by a separation of the exchanged

12 o be inhibited by 5-CHO-H(4)PteGlu(n) as are SHMTs from other organisms.

13 alciparum (Pf) and Arabidopsis thaliana (At) SHMT in target assays and PfNF54 strains in cell-based a

14 ed into a rapid and sensitive assay for both SHMT and H4PteGlun and the one-carbon derivatives of H4P

15 for folate-dependent reactions catalyzed by SHMT.

16 In this method, serine formed by SHMT activity is reacted with 4-fluoro-7-nitro-2,1,3-ben

17 ofolate is a property of other characterized SHMTs.

18 in strains lacking SHMT activity, confirming SHMT as the in vivo source of 5-CHO-THF.

19 Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon s

20 es cerevisiae, mitochondrial and cytoplasmic SHMT isozymes are encoded by distinct nuclear genes (SHM

21 e of the inactive form of murine cytoplasmic SHMT (cSHMT), lacking only the polyglutamate tail of the

22 ture at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two forms: one with the PLP covalently

23 ydropteroylpolyglutamate on rabbit cytosolic SHMT.

24 site mutant homotetrameric rabbit cytosolic SHMTs identified lysine residues that contribute to the

25 that lacks mitochondrial, but not cytosolic, SHMT activity.

26 teGlu5 has a 300-fold increased affinity for SHMT compared to 5-CHO-H4PteGlu.

27 not readily available for use in assays for SHMT activity.

28 n donor formate generally rescues cells from SHMT inhibition, but paradoxically increases the inhibit

29 ure closely resembles the structure of human SHMT, confirming its similarity to the alpha-class of PL

30 r measuring serine hydroxymethyltransferase (SHMT) activity toward formation of serine and (6S)-H(4)P

31 tochondrial serine hydroxymethyltransferase (SHMT) activity.

32 activity of serine hydroxymethyltransferase (SHMT) and strongly inhibits SHMT and other folate-depend

33 Serine hydroxymethyltransferase (SHMT) catalyzes the reversible and THF-dependent convers

34 Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to for

35 Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to gly

36 Serine hydroxymethyltransferase (SHMT) catalyzes the reversible interconversion of serine

37 Serine hydroxymethyltransferase (SHMT) from all sources tested catalyzes the slow exchang

38 Serine hydroxymethyltransferase (SHMT) from plant mitochondria was shown to be inhibited

39 MTHFD1) and serine hydroxymethyltransferase (SHMT) generate 5,10-methylenetetrahydrofolate for de nov

40 Serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme

41 Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent enzyme that cat

42 Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enz

43 Serine hydroxymethyltransferase (SHMT) is the major provider of one-carbon units in the c

44 richia coli serine hydroxymethyltransferase (SHMT) showed that the final rate determining folding ste

45 r cytosolic serine hydroxymethyltransferase (SHMT) were determined by a combination of isothermal tit

46 se (MTHFR), serine hydroxymethyltransferase (SHMT), and cystathionine beta-synthase (CBS) genes and t

47 tochondrial serine hydroxymethyltransferase (SHMT), combined with glycine decarboxylase, catalyzes an

48 the enzyme serine hydroxymethyltransferase (SHMT), designed to improve microsomal metabolic stabilit

49 theless for serine hydroxymethyltransferase (SHMT), one of the key enzymes of this cycle, efficient i

50 the enzymes serine hydroxymethyltransferase (SHMT), thymidylate synthase (TYMS), and dihydrofolate re

51 nhibitor of serine hydroxymethyltransferase (SHMT), was enriched in nuclei, accounting for 35% of fol

52 atalyzed by serine hydroxymethyltransferase (SHMT).

53 Serine hydroxymethyltransferase (SHMT; EC 2.1.2.1) catalyzes the reversible interconversi

54 cytosolic serine hydroxymethyltransferases (SHMT) confirmed their close similarity in tertiary and d

55 ne or both serine hydroxymethyltransferases (SHMT) or at the genes encoding one or both methylenetetr

56 The enzyme serine hydroxymethyltransferse (SHMT) converts serine into glycine and a tetrahydrofolat

57 midylate (dTMP) synthesis through changes in SHMT expression is causative in folate-responsive NTDs.

58 se data establish that 5-CHO-THF can inhibit SHMT in vivo and thereby influence glycine pool size.

59 thyltransferase (SHMT) and strongly inhibits SHMT and other folate-dependent enzymes in vitro.

60 -CHO-THF was undetectable in strains lacking SHMT activity, confirming SHMT as the in vivo source of

61 first structure of a ligand-bound mammalian SHMT allows identification of amino acid residues involv

62 Mitochondrial SHMT mRNA levels in MCF-7 cells did not vary during the

63 is mitochondrial in plants and mitochondrial SHMT is central to photorespiration, we examined the imp

64 present in eukaryotic cells as mitochondrial SHMT and cytoplasmic (cSHMT) isozymes that are encoded b

65 lly conserved within the human mitochondrial SHMT gene.

66 gnated shm1-1) is defective in mitochondrial SHMT activity and displays a lethal photorespiratory phe

67 Since mitochondrial SHMT is crucial to photorespiration, 5-FCL may help prev

68 This study suggests that mitochondrial SHMT-derived one-carbon units are essential for folate-m

69 and glycine were present, the mitochondrial SHMT made a significant contribution of one-carbon units

70 ffects SHM1, which encodes the mitochondrial SHMT required for photorespiration.

71 When grown on glycine, the mitochondrial SHMT was the predominant isozyme catalyzing the synthesi

72 Analyzed by the single-hit multitarget (SHMT) model, F1, F5, and F7, like camptothecin, induce R

73 both a Gly and Ala residue, and each mutant SHMT was purified and characterized with respect to kine

74 s in its configuration, and the P258A mutant SHMT showed reduced thermal stability.

75 No SHMT has been purified from a nonmethanogenic Archaea st

76 xplaining previous observations that nuclear SHMT is not a robust source of one-carbons for de novo d

77 bes the purification and characterization of SHMT from the thermophilic organism Sulfolobus solfatari

78 In the presence of an excess of SHMT the exchange rate is directly proportional to the c

79 in maintaining the structure and function of SHMT and a possible role in pyridoxal 5'-phosphate addit

80 Glu75 of SHMT is clearly involved in the reaction mechanism; it i

81 estigation on species-specific inhibition of SHMT for antimalarial drug development.

82 e rate is proportional to nanogram levels of SHMT.

83 ns the properties of several site mutants of SHMT and offers testable hypotheses for a more detailed

84 Studies of wild-type and site mutants of SHMT have failed to clearly establish the mechanism of t

85 upplemented media indicated that the role of SHMT in the KinB pathway is to feed the pool of C1 units

86 ycine formation is the rate-limiting step of SHMT catalysis.

87 ation significantly changed the structure of SHMT, the spectral properties of its complexes, or the k

88 ificant similarity with those of peptides of SHMTs from two methanogens.

89 that only two of the four catalytic sites on SHMT are catalytically competent and that the cSHMT-glyc

90 s and complex formation for photorespiratory SHMT activity demonstrates more complicated regulation o

91 nteraction is necessary for photorespiratory SHMT activity.

92 a pyrazolopyran scaffold that inhibits plant SHMT, we identify small-molecule dual inhibitors of huma

93 On the basis of plant SHMT inhibitors from an herbicide optimization program,

94 um falciparum (Pf) and Plasmodium vivax (Pv) SHMT with a pyrazolopyran core structure were identified

95 co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, in

96 n 6 genes (MTHFR, MTRR, FOLH1, CbetaS, RFC1, SHMT) involved in folate absorption and metabolism were

97 nism for previous studies demonstrating that SHMT expression is rate-limiting for de novo thymidylate

98 thase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for co

99 Mapping of the identified mutations onto the SHMT structural model uncovered key residues for structu

100 In addition, this SHMT also catalyzed the cleavage of both allo-threonine

101 THF levels do not much affect fluxes through SHMT or any other folate-dependent reaction, i.e. that 5

102 tive inhibitors of 5-CHO-H4PteGlu binding to SHMT, showing that anions compete for the polyglutamate

103 Binding of 5-CHO-H4PteGlun to SHMT exhibits both positive enthalpy and entropy, showin

104 ives of 5-CHO-H4PteGlun were cross-linked to SHMT by a carbodiimide reaction to Lys-450 which resides

105 t B-cell lines are particularly sensitive to SHMT inhibition.

106 coding the serine hydroxymethyl transferase (SHMT).

107 to investigate the contributions of the two SHMT isozymes to the production of glycine and one-carbo

108 ines, rendering them uniquely dependent upon SHMT enzymatic activity to meet glycine demand.

109 drofolate in complexes of these species with SHMT.