PMID- 4622901
OWN - NLM
STAT- MEDLINE
DCOM- 19720620
LR  - 20210526
IS  - 0021-9193 (Print)
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Linking)
VI  - 110
IP  - 1
DP  - 1972 Apr
TI  - Initiation of spore germination in glycolytic mutants of Bacillus subtilis.
PG  - 321-8
AB  - Enzyme activities of glycolysis and glyconeogenesis are present in spores of 
      Bacillus subtilis, the rate-limiting step of glucose (GLC) metabolism being its 
      phosphorylation. GLC allows initiation of germination in the presence of fructose 
      (FRU) and asparagine (ASN), not because it is used via the Embden-Meyerhof path, 
      but because it is oxidized in the nonphosphorylated form via the spore-specific 
      GLC dehydrogenase. Spores of mutants lacking GLC-phosphoenolpyruvate transferase, 
      FRU-6-P-kinase, or phosphoglucoisomerase activity can still be initiated by the 
      above substrate combination. Furthermore, GLC can be replaced by 2-deoxy-GLC, 
      which is also oxidized by GLC-dehydrogenase, but not by alpha- or 
      beta-methylglucoside, which are not substrates of this enzyme. GLC probably acts 
      by reducing nicotinamide adenine dinucleotide (or nicotinamide adenine 
      dinucleotide phosphate), which is used for some metabolic reaction other than the 
      cytochrome-linked electron transport system, since inhibitors of this system do 
      not inhibit initiation. Spores of a mutant lacking FRU-1-P-kinase activity can no 
      longer be initiated by GLC+FRU+ASN, but they do respond to the combination of 
      GLC+mannose+ASN. Since spores of a FRU-6-P-kinase (or phosphoglucoisomerase) 
      mutant can still respond to either FRU or mannose, FRU-6-P (or some derivative) 
      apparently is needed for initiation (in addition to reduced nicotinamide adenine 
      dinucleotide and an amino donor). Alanine can initiate germination in spores of 
      all of the above mutants, indicating that it can form all required compounds. 
      However, in a mutant lacking P-glycerate kinase activity, alanine initiates only 
      after a long lag and at a slow rate, indicating that some compound in the upper 
      metabolic subdivision is required for initiation, in agreement with the above 
      findings. All initiating agents of B. subtilis probably produce the same required 
      compound(s) by different metabolic routes.
FAU - Prasad, C
AU  - Prasad C
FAU - Diesterhaft, M
AU  - Diesterhaft M
FAU - Freese, E
AU  - Freese E
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Fructosephosphates)
RN  - 0 (Glycosides)
RN  - 0 (Hexoses)
RN  - 0 (Phosphorus Isotopes)
RN  - 30237-26-4 (Fructose)
RN  - 7006-34-0 (Asparagine)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 1.1.3.4 (Glucose Oxidase)
RN  - IY9XDZ35W2 (Glucose)
RN  - OF5P57N2ZX (Alanine)
RN  - PHA4727WTP (Mannose)
SB  - IM
MH  - Adenosine Triphosphate
MH  - Alanine/pharmacology
MH  - Asparagine/pharmacology
MH  - Bacillus subtilis/drug effects/enzymology/*growth & development/metabolism
MH  - Fructose/pharmacology
MH  - Fructosephosphates/pharmacology
MH  - Genetics, Microbial
MH  - Glucose/metabolism/*pharmacology
MH  - Glucose Oxidase
MH  - *Glycolysis
MH  - Glycosides/pharmacology
MH  - Hexoses/pharmacology
MH  - Mannose/pharmacology
MH  - Mutation
MH  - Phosphorus Isotopes
MH  - Spores/*growth & development
MH  - Spores, Bacterial/drug effects/enzymology/growth & development/metabolism
PMC - PMC247414
EDAT- 1972/04/01 00:00
MHDA- 1972/04/01 00:01
PMCR- 1972/04/01
CRDT- 1972/04/01 00:00
PHST- 1972/04/01 00:00 [pubmed]
PHST- 1972/04/01 00:01 [medline]
PHST- 1972/04/01 00:00 [entrez]
PHST- 1972/04/01 00:00 [pmc-release]
AID - 10.1128/jb.110.1.321-328.1972 [doi]
PST - ppublish
SO  - J Bacteriol. 1972 Apr;110(1):321-8. doi: 10.1128/jb.110.1.321-328.1972.