A mutant of Mycobacterium smegmatis defective in dipeptide transport

Achal Bhatt, Renee Green, Roswell Coles, Michael Condon, Nancy Connell

Research output: Contribution to journalArticle

Abstract

A mutant of Mycobacterium smegmatis unable to use the dipeptide carnosine (β-alanyl-L-histidine) as a sole carbon or nitrogen source was isolated. Carnosinase activity and the ability to grow on β-Ala and/or L- His were similar in the mutant and the wild type. However, the mutant showed significant impairment in the uptake of camosine. This study is the first description of a peptide utilization mutant of a mycobacterium.

Original languageEnglish (US)
Pages (from-to)6773-6775
Number of pages3
JournalJournal of Bacteriology
Volume180
Issue number24
StatePublished - Dec 1 1998
Externally publishedYes

Fingerprint

Carnosine
Mycobacterium smegmatis
Dipeptides
Mycobacterium
Histidine
Nitrogen
Carbon
Peptides
aminoacyl-histidine dipeptidase

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Bhatt, A., Green, R., Coles, R., Condon, M., & Connell, N. (1998). A mutant of Mycobacterium smegmatis defective in dipeptide transport. Journal of Bacteriology, 180(24), 6773-6775.

A mutant of Mycobacterium smegmatis defective in dipeptide transport. / Bhatt, Achal; Green, Renee; Coles, Roswell; Condon, Michael; Connell, Nancy.

In: Journal of Bacteriology, Vol. 180, No. 24, 01.12.1998, p. 6773-6775.

Research output: Contribution to journalArticle

Bhatt, A, Green, R, Coles, R, Condon, M & Connell, N 1998, 'A mutant of Mycobacterium smegmatis defective in dipeptide transport', Journal of Bacteriology, vol. 180, no. 24, pp. 6773-6775.
Bhatt A, Green R, Coles R, Condon M, Connell N. A mutant of Mycobacterium smegmatis defective in dipeptide transport. Journal of Bacteriology. 1998 Dec 1;180(24):6773-6775.
Bhatt, Achal ; Green, Renee ; Coles, Roswell ; Condon, Michael ; Connell, Nancy. / A mutant of Mycobacterium smegmatis defective in dipeptide transport. In: Journal of Bacteriology. 1998 ; Vol. 180, No. 24. pp. 6773-6775.
@article{3ff462a2526d45b89f8acd5e74b4a50d,
title = "A mutant of Mycobacterium smegmatis defective in dipeptide transport",
abstract = "A mutant of Mycobacterium smegmatis unable to use the dipeptide carnosine (β-alanyl-L-histidine) as a sole carbon or nitrogen source was isolated. Carnosinase activity and the ability to grow on β-Ala and/or L- His were similar in the mutant and the wild type. However, the mutant showed significant impairment in the uptake of camosine. This study is the first description of a peptide utilization mutant of a mycobacterium.",
author = "Achal Bhatt and Renee Green and Roswell Coles and Michael Condon and Nancy Connell",
year = "1998",
month = "12",
day = "1",
language = "English (US)",
volume = "180",
pages = "6773--6775",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "24",

}

TY - JOUR

T1 - A mutant of Mycobacterium smegmatis defective in dipeptide transport

AU - Bhatt, Achal

AU - Green, Renee

AU - Coles, Roswell

AU - Condon, Michael

AU - Connell, Nancy

PY - 1998/12/1

Y1 - 1998/12/1

N2 - A mutant of Mycobacterium smegmatis unable to use the dipeptide carnosine (β-alanyl-L-histidine) as a sole carbon or nitrogen source was isolated. Carnosinase activity and the ability to grow on β-Ala and/or L- His were similar in the mutant and the wild type. However, the mutant showed significant impairment in the uptake of camosine. This study is the first description of a peptide utilization mutant of a mycobacterium.

AB - A mutant of Mycobacterium smegmatis unable to use the dipeptide carnosine (β-alanyl-L-histidine) as a sole carbon or nitrogen source was isolated. Carnosinase activity and the ability to grow on β-Ala and/or L- His were similar in the mutant and the wild type. However, the mutant showed significant impairment in the uptake of camosine. This study is the first description of a peptide utilization mutant of a mycobacterium.

UR - http://www.scopus.com/inward/record.url?scp=0032444548&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032444548&partnerID=8YFLogxK

M3 - Article

C2 - 9852030

AN - SCOPUS:0032444548

VL - 180

SP - 6773

EP - 6775

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 24

ER -