Literature DB >> 6363292

Peptide utilization by oral streptococci.

C Andersson, M L Sund, L Linder.   

Abstract

Streptococcus mitis ATCC 903 and Streptococcus sanguis 804 could utilize large peptides present in proteose peptone as their sole source of nitrogen but grew poorly in amino acid medium. By contrast, Streptococcus mutans BHT and S. mutans IB grew in amino acid medium but could not utilize large peptides. Streptococcus sp. strain Bravato had requirements for both peptides and amino acids. Peptide size did not seem important for the utilization of peptides by S. mitis except that dipeptides were not utilized. Large peptides were essential for depressed hyaluronidase synthesis in nongrowing S. mitis. Intracellular aminopeptidase activities were high in S. mitis ATCC 903 and Streptococcus sp. strain Bravato, intermediate in S. sanguis 804, and low in S. mutans BHT and S. mutans IB.

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Year:  1984        PMID: 6363292      PMCID: PMC264333          DOI: 10.1128/iai.43.2.555-560.1984

Source DB:  PubMed          Journal:  Infect Immun        ISSN: 0019-9567            Impact factor:   3.441


  17 in total

1.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

2.  Utilization of methionine-containing peptides and their derivatives by a methionine-requiring auxotroph of Saccharomyces cerevisiae.

Authors:  F Naider; J M Becker; E Katzir-Katchalski
Journal:  J Biol Chem       Date:  1974-01-10       Impact factor: 5.157

3.  Formation and release of hyaluronidase and aminopeptidase in non-growing cells of Streptococcus mitis, ATCC 903.

Authors:  L Linder
Journal:  Acta Pathol Microbiol Scand B Microbiol Immunol       Date:  1974-10

4.  Estimation of cell lysis. Determination of aminopeptidase in extracts of Streptococcus mitis, ATCC 903.

Authors:  L Linder; L Lindquist; P O Söder; T Holme
Journal:  Acta Pathol Microbiol Scand B Microbiol Immunol       Date:  1974-10

5.  Extraction of cell-bound hyaluronidase and aminopeptidase from Streptococcus mitis, ATCC 903.

Authors:  L Linder
Journal:  Acta Pathol Microbiol Scand B Microbiol Immunol       Date:  1974-10

6.  Hyaluronidase and aminopeptidase activity in cultures of streptococcus mitis, ATCC 903.

Authors:  L Linder; T Holme; G Frostell
Journal:  Acta Pathol Microbiol Scand B Microbiol Immunol       Date:  1974-08

7.  Size restriction on peptide utilization in Escherichia coli.

Authors:  J W Payne; C Gilvarg
Journal:  J Biol Chem       Date:  1968-12-10       Impact factor: 5.157

8.  [Effect of glucagon peptide fragments in relation to growth of Streptococcus thermophilus].

Authors:  M J Desmazeaud; J H Hermier
Journal:  Biochimie       Date:  1973       Impact factor: 4.079

9.  Amino acid and peptide requirement of Fusiformis necrophorus.

Authors:  A Wahren; T Holme
Journal:  J Bacteriol       Date:  1973-10       Impact factor: 3.490

10.  PEPTIDES AND OTHER NITROGEN SOURCES FOR GROWTH OF BACTEROIDES RUMINICOLA.

Authors:  K A PITTMAN; M P BRYANT
Journal:  J Bacteriol       Date:  1964-08       Impact factor: 3.490

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  5 in total

1.  Response of a Streptococcus sanguis strain to arginine-containing peptides.

Authors:  A H Rogers; P S Zilm; N J Gully; A L Pfennig
Journal:  Infect Immun       Date:  1988-03       Impact factor: 3.441

2.  Extracellular arginine aminopeptidase from Streptococcus gordonii FSS2.

Authors:  J M Goldstein; D Nelson; T Kordula; J A Mayo; J Travis
Journal:  Infect Immun       Date:  2002-02       Impact factor: 3.441

3.  Novel extracellular x-prolyl dipeptidyl-peptidase (DPP) from Streptococcus gordonii FSS2: an emerging subfamily of viridans Streptococcal x-prolyl DPPs.

Authors:  J M Goldstein; A Banbula; T Kordula; J A Mayo; J Travis
Journal:  Infect Immun       Date:  2001-09       Impact factor: 3.441

4.  Comparison of aminopeptidase activities in four strains of mutans group oral streptococci.

Authors:  R A Cowman; S S Baron
Journal:  Infect Immun       Date:  1993-01       Impact factor: 3.441

5.  SO-LAAO, a novel L-amino acid oxidase that enables Streptococcus oligofermentans to outcompete Streptococcus mutans by generating H2O2 from peptone.

Authors:  Huichun Tong; Wei Chen; Wenyuan Shi; Fengxia Qi; Xiuzhu Dong
Journal:  J Bacteriol       Date:  2008-05-09       Impact factor: 3.490

  5 in total

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